{"PubmedArticle":{"MedlineCitation":{"@attributes":{"Status":"MEDLINE","Owner":"NLM","IndexingMethod":"Curated"},"PMID":{"@attributes":{"Version":"1"},"@text":"39663450"},"DateCompleted":{"Year":"2025","Month":"04","Day":"27"},"DateRevised":{"Year":"2026","Month":"05","Day":"16"},"Article":{"@attributes":{"PubModel":"Print-Electronic"},"Journal":{"ISSN":{"@attributes":{"IssnType":"Electronic"},"@text":"1476-4687"},"JournalIssue":{"@attributes":{"CitedMedium":"Internet"},"Volume":"637","Issue":"8048","PubDate":{"Year":"2025","Month":"Jan"}},"Title":"Nature","ISOAbbreviation":"Nature"},"ArticleTitle":"Structure and assembly of the dystrophin glycoprotein complex.","Pagination":{"StartPage":"1252","EndPage":"1260","MedlinePgn":"1252-1260"},"ELocationID":[{"@attributes":{"EIdType":"doi","ValidYN":"Y"},"@text":"10.1038\/s41586-024-08310-2"}],"Abstract":{"AbstractText":["The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular matrix<sup>1-3<\/sup>. Dysfunction of dystrophin and its associated proteins results in muscular dystrophy, a disorder characterized by progressive muscle weakness and degeneration<sup>4,5<\/sup>. Despite the important roles of the DGC in physiology and pathology, its structural details remain largely unknown, hindering a comprehensive understanding of its assembly and function. Here we isolated the native DGC from mouse skeletal muscle and obtained its high-resolution structure. Our findings unveil a markedly divergent structure from the previous model of DGC assembly. Specifically, on the extracellular side, \u03b2-, \u03b3- and \u03b4-sarcoglycans co-fold to form a specialized, extracellular tower-like structure, which has a central role in complex assembly by providing binding sites for \u03b1-sarcoglycan and dystroglycan. In the transmembrane region, sarcoglycans and sarcospan flank and stabilize the single transmembrane helix of dystroglycan, rather than forming a subcomplex as previously proposed<sup>6-8<\/sup>. On the intracellular side, sarcoglycans and dystroglycan engage in assembly with the dystrophin-dystrobrevin subcomplex through extensive interaction with the ZZ domain of dystrophin. Collectively, these findings enhance our understanding of the structural linkage across the cell membrane and provide a foundation for the molecular interpretation of many muscular dystrophy-related mutations."],"CopyrightInformation":"\u00a9 2024. The Author(s), under exclusive licence to Springer Nature Limited."},"AuthorList":{"@attributes":{"CompleteYN":"Y"},"Author":[{"@attributes":{"ValidYN":"Y","EqualContrib":"Y"},"LastName":"Wan","ForeName":"Li","Initials":"L","AffiliationInfo":[{"Affiliation":"Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China."},{"Affiliation":"Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China."},{"Affiliation":"Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, China."}]},{"@attributes":{"ValidYN":"Y","EqualContrib":"Y"},"LastName":"Ge","ForeName":"Xiaofei","Initials":"X","Identifier":[{"@attributes":{"Source":"ORCID"},"@text":"0009-0005-9626-7061"}],"AffiliationInfo":[{"Affiliation":"State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China."}]},{"@attributes":{"ValidYN":"Y","EqualContrib":"Y"},"LastName":"Xu","ForeName":"Qikui","Initials":"Q","AffiliationInfo":[{"Affiliation":"Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China."},{"Affiliation":"Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China."},{"Affiliation":"Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, China."}]},{"@attributes":{"ValidYN":"Y","EqualContrib":"Y"},"LastName":"Huang","ForeName":"Gaoxingyu","Initials":"G","AffiliationInfo":[{"Affiliation":"Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China."},{"Affiliation":"Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China."},{"Affiliation":"Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, China."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Yang","ForeName":"Tiandi","Initials":"T","AffiliationInfo":[{"Affiliation":"Howard Hughes Medical Institute, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Senator Paul D. Wellstone Muscular Dystrophy Specialized Research Center, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Department of Molecular Physiology and Biophysics, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Department of Neurology, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Department of Immunology, Harvard Medical School, Boston, MA, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Campbell","ForeName":"Kevin P","Initials":"KP","Identifier":[{"@attributes":{"Source":"ORCID"},"@text":"0000-0003-2066-5889"}],"AffiliationInfo":[{"Affiliation":"Howard Hughes Medical Institute, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Senator Paul D. Wellstone Muscular Dystrophy Specialized Research Center, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Department of Molecular Physiology and Biophysics, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."},{"Affiliation":"Department of Neurology, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Yan","ForeName":"Zhen","Initials":"Z","Identifier":[{"@attributes":{"Source":"ORCID"},"@text":"0000-0002-1999-8451"}],"AffiliationInfo":[{"Affiliation":"Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China. yanzhen@westlake.edu.cn."},{"Affiliation":"Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China. yanzhen@westlake.edu.cn."},{"Affiliation":"Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, China. yanzhen@westlake.edu.cn."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Wu","ForeName":"Jianping","Initials":"J","Identifier":[{"@attributes":{"Source":"ORCID"},"@text":"0000-0001-9869-7691"}],"AffiliationInfo":[{"Affiliation":"Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China. wujianping@westlake.edu.cn."},{"Affiliation":"Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, China. wujianping@westlake.edu.cn."},{"Affiliation":"Institute of Biology, Westlake Institute for Advanced Study, Hangzhou, China. wujianping@westlake.edu.cn."}]}]},"Language":["eng"],"GrantList":{"@attributes":{"CompleteYN":"Y"},"Grant":[{"GrantID":"P50 NS053672","Acronym":"NS","Agency":"NINDS NIH HHS","Country":"United States"}]},"PublicationTypeList":{"PublicationType":[{"@attributes":{"UI":"D016428"},"@text":"Journal Article"},{"@attributes":{"UI":"D052061"},"@text":"Research Support, N.I.H., Extramural"},{"@attributes":{"UI":"D013485"},"@text":"Research Support, Non-U.S. Gov't"}]},"ArticleDate":[{"@attributes":{"DateType":"Electronic"},"Year":"2024","Month":"12","Day":"11"}]},"MedlineJournalInfo":{"Country":"England","MedlineTA":"Nature","NlmUniqueID":"0410462","ISSNLinking":"0028-0836"},"ChemicalList":{"Chemical":[{"RegistryNumber":"146888-27-9","NameOfSubstance":{"@attributes":{"UI":"D049030"},"@text":"Dystroglycans"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D016189"},"@text":"Dystrophin"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D049031"},"@text":"Sarcoglycans"}}]},"CitationSubset":["IM"],"MeshHeadingList":{"MeshHeading":[{"DescriptorName":{"@attributes":{"UI":"D000818","MajorTopicYN":"N"},"@text":"Animals"}},{"DescriptorName":{"@attributes":{"UI":"D051379","MajorTopicYN":"N"},"@text":"Mice"}},{"DescriptorName":{"@attributes":{"UI":"D001665","MajorTopicYN":"N"},"@text":"Binding Sites"}},{"DescriptorName":{"@attributes":{"UI":"D020285","MajorTopicYN":"N"},"@text":"Cryoelectron Microscopy"}},{"DescriptorName":{"@attributes":{"UI":"D049030","MajorTopicYN":"Y"},"@text":"Dystroglycans"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"N"},"@text":"chemistry"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"},{"@attributes":{"UI":"Q000648","MajorTopicYN":"N"},"@text":"ultrastructure"}]},{"DescriptorName":{"@attributes":{"UI":"D016189","MajorTopicYN":"Y"},"@text":"Dystrophin"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"N"},"@text":"chemistry"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"},{"@attributes":{"UI":"Q000648","MajorTopicYN":"N"},"@text":"ultrastructure"}]},{"DescriptorName":{"@attributes":{"UI":"D008958","MajorTopicYN":"N"},"@text":"Models, Molecular"}},{"DescriptorName":{"@attributes":{"UI":"D018482","MajorTopicYN":"N"},"@text":"Muscle, Skeletal"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"N"},"@text":"chemistry"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"}]},{"DescriptorName":{"@attributes":{"UI":"D011485","MajorTopicYN":"N"},"@text":"Protein Binding"}},{"DescriptorName":{"@attributes":{"UI":"D049031","MajorTopicYN":"Y"},"@text":"Sarcoglycans"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"N"},"@text":"chemistry"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"},{"@attributes":{"UI":"Q000648","MajorTopicYN":"N"},"@text":"ultrastructure"}]}]},"CoiStatement":"Competing interests: The authors declare no competing interests."},"PubmedData":{"History":{"PubMedPubDate":[{"@attributes":{"PubStatus":"received"},"Year":"2024","Month":"6","Day":"13"},{"@attributes":{"PubStatus":"accepted"},"Year":"2024","Month":"10","Day":"30"},{"@attributes":{"PubStatus":"medline"},"Year":"2025","Month":"1","Day":"30","Hour":"0","Minute":"19"},{"@attributes":{"PubStatus":"pubmed"},"Year":"2024","Month":"12","Day":"12","Hour":"0","Minute":"24"},{"@attributes":{"PubStatus":"entrez"},"Year":"2024","Month":"12","Day":"11","Hour":"23","Minute":"30"},{"@attributes":{"PubStatus":"pmc-release"},"Year":"2026","Month":"5","Day":"15"}]},"PublicationStatus":"ppublish","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"39663450"},{"@attributes":{"IdType":"mid"},"@text":"NIHMS2116392"},{"@attributes":{"IdType":"pmc"},"@text":"PMC13178787"},{"@attributes":{"IdType":"doi"},"@text":"10.1038\/s41586-024-08310-2"},{"@attributes":{"IdType":"pii"},"@text":"10.1038\/s41586-024-08310-2"}]},"ReferenceList":[{"Reference":[{"Citation":"Campbell KP &amp; Kahl SD Association of dystrophin and an integral membrane glycoprotein. Nature 338, 259\u2013262 (1989).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"2493582"}]}},{"Citation":"Ibraghimov-Beskrovnaya O et al. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355, 696\u2013702 (1992).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"1741056"}]}},{"Citation":"Ervasti JM &amp; Campbell KP A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol 122, 809\u2013823 (1993).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2119587"},{"@attributes":{"IdType":"pubmed"},"@text":"8349731"}]}},{"Citation":"McNally EM &amp; Pytel P Muscle diseases: the muscular dystrophies. Annu. Rev. Pathol 2, 87\u2013109 (2007).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"18039094"}]}},{"Citation":"Duan DS, Goemans N, Takeda S, Mercuri E &amp; Aartsma-Rus A Duchenne muscular dystrophy. Nat. Rev. Dis. Primers 7, 13 (2021).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC10557455"},{"@attributes":{"IdType":"pubmed"},"@text":"33602943"}]}},{"Citation":"Durbeej M &amp; Campbell KP Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr. Opin. Genet. Dev 12, 349\u2013361 (2002).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12076680"}]}},{"Citation":"Wilson DGS, Tinker A &amp; Iskratsch T The role of the dystrophin glycoprotein complex in muscle cell mechanotransduction. Commun. Biol 5, 1022 (2022).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC9515174"},{"@attributes":{"IdType":"pubmed"},"@text":"36168044"}]}},{"Citation":"Gao QQ &amp; McNally EM The dystrophin complex: structure, function, and implications for therapy. Compr. Physiol 5, 1223\u20131239 (2015).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4767260"},{"@attributes":{"IdType":"pubmed"},"@text":"26140716"}]}},{"Citation":"Gumerson JD &amp; Michele DE The dystrophin-glycoprotein complex in the prevention of muscle damage. J. Biomed. Biotechnol 2011, 210797 (2011).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3189583"},{"@attributes":{"IdType":"pubmed"},"@text":"22007139"}]}},{"Citation":"Lapidos KA, Kakkar R &amp; McNally EM The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma. Circ. Res 94, 1023\u20131031 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15117830"}]}},{"Citation":"Belhasan DC &amp; Akaaboune M The role of the dystrophin glycoprotein complex on the neuromuscular system. Neurosci. Lett 722, 134833 (2020).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC8792866"},{"@attributes":{"IdType":"pubmed"},"@text":"32057921"}]}},{"Citation":"Pilgram GSK, Potikanond S, Baines RA, Fradkin LG &amp; Noordermeer JN The roles of the dystrophin-associated glycoprotein complex at the synapse. Mol. Neurobiol 41, 1\u201321 (2010).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2840664"},{"@attributes":{"IdType":"pubmed"},"@text":"19899002"}]}},{"Citation":"Constantin B Dystrophin complex functions as a scaffold for signalling proteins. Boichim. Biophys. Acta 1838, 635\u2013642 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"24021238"}]}},{"Citation":"Hoffman EP, Brown RH &amp; Kunkel LM Dystrophin\u2014the protein product of the Duchenne muscular-dystrophy locus. Cell 51, 919\u2013928 (1987).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"3319190"}]}},{"Citation":"Koenig M, Monaco AP &amp; Kunkel LM The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53, 219\u2013228 (1988).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"3282674"}]}},{"Citation":"Rybakova IN, Patel JR &amp; Ervasti JM The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol 150, 1209\u20131214 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2175263"},{"@attributes":{"IdType":"pubmed"},"@text":"10974007"}]}},{"Citation":"Bhat HF et al. ABC of multifaceted dystrophin glycoprotein complex (DGC). J. Cell. Physiol 233, 5142\u20135159 (2018).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"28464259"}]}},{"Citation":"Deyst KA, Bowe MA, Leszyk JD &amp; Fallon JR The \u03b1-dystroglycan-\u03b2-dystroglycan complex. Membrane organization and relationship to an agrin receptor. J. Biol. Chem 270, 25956\u201325959 (1995).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"7592785"}]}},{"Citation":"Holt KH, Crosbie RH, Venzke DP &amp; Campbell KP Biosynthesis of dystroglycan: processing of a precursor propeptide. FEBS Lett. 468, 79\u201383 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10683445"}]}},{"Citation":"Martin PT Dystroglycan glycosylation and its role in matrix binding in skeletal muscle. Glycobiology 13, 55R\u201366R (2003).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12736199"}]}},{"Citation":"Sciandra F et al. Identification of the \u03b2-dystroglycan binding epitope within the C-terminal region of \u03b1-dystroglycan. Eur. J. Biochem 268, 4590\u20134597 (2001).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"11502221"}]}},{"Citation":"Crosbie RH, Heighway J, Venzke DP, Lee JC &amp; Campbell KP Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex. J. Biol. Chem 272, 31221\u201331224 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9395445"}]}},{"Citation":"Wein N, Alfano L &amp; Flanigan KM Genetics and emerging treatments for Duchenne and Becker muscular dystrophy. Pediatr. Clin. North. Am 62, 723\u2013742 (2015).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"26022172"}]}},{"Citation":"Mah JK et al. A systematic review and meta-analysis on the epidemiology of Duchenne and Becker muscular dystrophy. Neuromuscular Disord 24, 482\u2013491 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"24780148"}]}},{"Citation":"Nigro V &amp; Savarese M Genetic basis of limb-girdle muscular dystrophies: the 2014 update. Acta Myol 33, 1\u201312 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4021627"},{"@attributes":{"IdType":"pubmed"},"@text":"24843229"}]}},{"Citation":"Brown SC et al. Abnormalities in alpha-dystroglycan expression in MDC1C and LGMD2I muscular dystrophies. Am. J. Pathol 164, 727\u2013737 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1602276"},{"@attributes":{"IdType":"pubmed"},"@text":"14742276"}]}},{"Citation":"Michele DE et al. Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418, 417\u2013422 (2002).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12140558"}]}},{"Citation":"Barresi R &amp; Campbell KP Dystroglycan: from biosynthesis to pathogenesis of human disease. J. Cell Sci 119, 199\u2013207 (2006).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"16410545"}]}},{"Citation":"Waite A, Brown SC &amp; Blake DJ The dystrophin-glycoprotein complex in brain development and disease. Trends Neurosci. 35, 487\u2013496 (2012).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"22626542"}]}},{"Citation":"Tsubata S et al. Mutations in the human \u03b4-sarcoglycan gene in familial and sporadic dilated cardiomyopathy. J. Clin. Invest 106, 655\u2013662 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC381284"},{"@attributes":{"IdType":"pubmed"},"@text":"10974018"}]}},{"Citation":"Guiraud S et al. The pathogenesis and therapy of muscular dystrophies. Annu. Rev. Genomics Hum. Genet 16, 281\u2013308 (2015).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"26048046"}]}},{"Citation":"Norwood FLM, Sutherland-Smith AJ, Keep NH &amp; Kendrick-Jones J The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Structure 8, 481\u2013491 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10801490"}]}},{"Citation":"Muthu M, Richardson KA &amp; Sutherland-Smith AJ The crystal structures of dystrophin and utrophin spectrin repeats: implications for domain boundaries. PLoS ONE 7, e40066 (2012).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3401230"},{"@attributes":{"IdType":"pubmed"},"@text":"22911693"}]}},{"Citation":"Huang X et al. Structure of a WW domain containing fragment of dystrophin in complex with \u03b2-dystroglycan. Nat. Struct. Biol 7, 634\u2013638 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10932245"}]}},{"Citation":"Bozic D, Sciandra F, Lamba D &amp; Brancaccio A The structure of the N-terminal region of murine skeletal muscle \u03b1-dystroglycan discloses a modular architecture. J. Biol. Chem 279, 44812\u201344816 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15326183"}]}},{"Citation":"Briggs DC et al. Structural basis of laminin binding to the LARGE glycans on dystroglycan. Nat. Chem. Biol 12, 810\u2013814 (2016).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC5030134"},{"@attributes":{"IdType":"pubmed"},"@text":"27526028"}]}},{"Citation":"Ramaswamy KS et al. Lateral transmission of force is impaired in skeletal muscles of dystrophic mice and very old rats. J. Physiol 589, 1195\u20131208 (2011).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3060596"},{"@attributes":{"IdType":"pubmed"},"@text":"21224224"}]}},{"Citation":"Singh J et al. Proteolytic enzymes and altered glycosylation modulate dystroglycan function in carcinoma cells. Cancer Res. 64, 6152\u20136159 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15342399"}]}},{"Citation":"Jung D, Yang B, Meyer J, Chamberlain JS &amp; Campbell KP Identification and characterization of the dystrophin anchoring site on beta-dystroglycan. J. Biol. Chem 270, 27305\u201327310 (1995).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"7592992"}]}},{"Citation":"Chan YM &amp; Kunkel LM In vitro expressed dystrophin fragments do not associate with each other. FEBS Lett. 410, 153\u2013159 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9237620"}]}},{"Citation":"SadouletPuccio HM, Rajala M &amp; Kunkel LM Dystrobrevin and dystrophin: An interaction through coiled-coil motifs. Proc. Natl Acad. Sci. USA 94, 12413\u201312418 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC24974"},{"@attributes":{"IdType":"pubmed"},"@text":"9356463"}]}},{"Citation":"Swiderski K et al. Phosphorylation within the cysteine-rich region of dystrophin enhances its association with \u03b2-dystroglycan and identifies a potential novel therapeutic target for skeletal muscle wasting. Hum. Mol. Genet 23, 6697\u20136711 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4245040"},{"@attributes":{"IdType":"pubmed"},"@text":"25082828"}]}},{"Citation":"Ilsley JL, Sudol M &amp; Winder SJ The interaction of dystrophin with \u03b2-dystroglycan is regulated by tyrosine phosphorylation. Cell Signal 13, 625\u2013632 (2001).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"11495720"}]}},{"Citation":"Ge X &amp; Wang JW Structural mechanism of bacteriophage lambda tail\u2019s interaction with the bacterial receptor. Nat. Commun 15, 4185 (2024).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC11101478"},{"@attributes":{"IdType":"pubmed"},"@text":"38760367"}]}},{"Citation":"Hynes RO Integrins: bidirectional, allosteric signaling machines. Cell 110, 673\u2013687 (2002).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12297042"}]}},{"Citation":"Luo BH, Carman CV &amp; Springer TA Structural basis of integrin regulation and signaling. Annu. Rev. Immunol 25, 619\u2013647 (2007).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1952532"},{"@attributes":{"IdType":"pubmed"},"@text":"17201681"}]}},{"Citation":"Guo C et al. Absence of \u03b17 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy. Hum. Mol. Genet 15, 989\u2013998 (2006).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"16476707"}]}},{"Citation":"Rooney JE et al. Severe muscular dystrophy in mice that lack dystrophin and \u03b17 integrin. J. Cell Sci 119, 2185\u20132195 (2006).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"16684813"}]}},{"Citation":"Hodges BL et al. Altered expression of the \u03b17\u03b21 integrin in human and murine muscular dystrophies. J. Cell Sci 110, 2873\u20132881 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9427295"}]}},{"Citation":"Marshall JL &amp; Crosbie-Watson RH Sarcospan: a small protein with large potential for Duchenne muscular dystrophy. Skelet. Muscle 3, 1 (2013).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3599653"},{"@attributes":{"IdType":"pubmed"},"@text":"23282144"}]}},{"Citation":"Yan Z et al. Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature 517, 50\u201355 (2015).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4338550"},{"@attributes":{"IdType":"pubmed"},"@text":"25517095"}]}},{"Citation":"Diniz G et al. Sarcolemmal alpha and gamma sarcoglycan protein deficiencies in Turkish siblings with a novel missense mutation in the alpha sarcoglycan gene. Pediatr. Neurol 50, 640\u2013647 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"24742800"}]}},{"Citation":"Duggan DJ et al. Mutations in the sarcoglycan genes in patients with myopathy. New Engl. J. Med 336, 618\u2013624 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9032047"}]}},{"Citation":"Piccolo F et al. Primary adhalinopathy\u2014a common-cause of autosomal recessive muscular-dystrophy of variable severity. Nat. Genet 10, 243\u2013245 (1995).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"7663524"}]}},{"Citation":"Carrie A et al. Mutational diversity and hot spots in the alpha-sarcoglycan gene in autosomal recessive muscular dystrophy (LGMD2D). J. Med. Genet 34, 470\u2013475 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1050969"},{"@attributes":{"IdType":"pubmed"},"@text":"9192266"}]}},{"Citation":"Saha M et al. Impact of PYROXD1 deficiency on cellular respiration and correlations with genetic analyses of limb-girdle muscular dystrophy in Saudi Arabia and Sudan. Physiol. Genomics 50, 929\u2013939 (2018).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC6293114"},{"@attributes":{"IdType":"pubmed"},"@text":"30345904"}]}},{"Citation":"Kawai H et al. Adhalin gene mutations in patients with autosomal recessive childhood onset muscular dystrophy with adhalin deficiency. J. Clin. Invest 96, 1202\u20131207 (1995).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC185739"},{"@attributes":{"IdType":"pubmed"},"@text":"7657792"}]}},{"Citation":"Duclos F et al. \u03b2-sarcoglycan: genomic analysis and identification of a novel missense mutation in the LGMD2E Amish isolate. Neuromusc. Disord 8, 30\u201338 (1998).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9565988"}]}},{"Citation":"dos Santos MR, Jorge P, Ribeiro EM, Pires MM &amp; Guimaraes A Noval mutation (Y184C) in exon 4 of the beta-sarcoglycan gene identified in a Portuguese patient. Mutations in brief no. 177. Hum. Mutat 12, 214\u2013215 (1998).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10660328"}]}},{"Citation":"Bonnemann CG et al. Genomic screening for beta-sarcoglycan gene mutations: Missense mutations may cause severe limb-girdle muscular dystrophy type 2E (LGMD 2E). Hum. Mol. Genet 5, 1953\u20131961 (1996).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8968749"}]}},{"Citation":"B\u00f6nnemann CG et al. LGMD 2E in Tunisia is caused by a homozygous missense mutation in \u03b2-sarcoglycan exon 3. Neuromusc. Disord 8, 193\u2013197 (1998).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9631401"}]}},{"Citation":"Vermeer S et al. Novel mutations in three patients with LGMD2C with phenotypic differences. Pediatr. Neurol 30, 291\u2013294 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15087111"}]}},{"Citation":"Nowak KJ et al. Severe \u03b3-sarcoglycanopathy caused by a novel missense mutation and a large deletion. Neuromusc. Disord 10, 100\u2013107 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10714584"}]}},{"Citation":"Crosbie RH et al. Molecular and genetic characterization of sarcospan:: insights into sarcoglycan\u2013sarcospan interactions. Hum. Mol. Genet 9, 2019\u20132027 (2000).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10942431"}]}},{"Citation":"Piccolo F et al. A founder mutation in the \u03b3-sarcoglycan gene of Gypsies possibly predating their migration out of India. Hum. Mol. Genet 5, 2019\u20132022 (1996).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8968757"}]}},{"Citation":"Duggan DJ et al. Mutations in the \u03b4-sarcoglycan gene are a rare cause of autosomal recessive limb-girdle muscular dystrophy (LGMD2). Neurogenetics 1, 49\u201358 (1997).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10735275"}]}},{"Citation":"Nigro V et al. Identification of a novel sarcoglycan gene at 5q33 encoding a sarcolemmal 35 kDa glycoprotein. Hum. Mol. Genet 5, 1179\u20131186 (1996).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8842738"}]}},{"Citation":"Moreira ES et al. A first missense mutation in the \u03b4 sarcoglycan gene associated with a severe phenotype and frequency of limb-girdle muscular dystrophy type 2 F (LGMD2F) in Brazilian sarcoglycanopathies. J. Med. Genet 35, 951\u2013953 (1998).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1051491"},{"@attributes":{"IdType":"pubmed"},"@text":"9832045"}]}},{"Citation":"Geis T et al. Homozygous dystroglycan mutation associated with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy. Neurogenetics 14, 205\u2013213 (2013).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"24052401"}]}},{"Citation":"Dai Y et al. Whole exome sequencing identified a novel DAG1 mutation in a patient with rare, mild and late age of onset muscular dystrophy-dystroglycanopathy. J. Cell. Mol. Med 23, 811\u2013818 (2019).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC6349151"},{"@attributes":{"IdType":"pubmed"},"@text":"30450679"}]}},{"Citation":"Feng J, Yan J, Buzin CH, Towbin JA &amp; Sommer SS Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy. Mol. Genet. Metab 77, 119\u2013126 (2002).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12359139"}]}},{"Citation":"Flanigan KM et al. Rapid direct sequence analysis of the dystrophin gene. Am. J. Hum. Genet 72, 931\u2013939 (2003).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1180355"},{"@attributes":{"IdType":"pubmed"},"@text":"12632325"}]}},{"Citation":"Vulin A et al. The ZZ domain of dystrophin in DMD: making sense of missense mutations. Hum. Mutat 35, 257\u2013264 (2014).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4145872"},{"@attributes":{"IdType":"pubmed"},"@text":"24302611"}]}},{"Citation":"Goldberg LR et al. A dystrophin missense mutation showing persistence of dystrophin and dystrophin-associated proteins yet a severe phenotype. Ann. Neurol 44, 971\u2013976 (1998).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9851445"}]}},{"Citation":"Lenk U et al. A cysteine 3340 substitution in the dystroglycan-binding domain of dystrophin associated with Duchenne muscular dystrophy, mental retardation and absence of the ERG b-wave. Hum. Mol. Genet 5, 973\u2013975 (1996).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8817332"}]}},{"Citation":"Zheng SQ et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331\u2013332 (2017).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC5494038"},{"@attributes":{"IdType":"pubmed"},"@text":"28250466"}]}},{"Citation":"Punjani A, Rubinstein JL, Fleet DJ &amp; Brubaker MA cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290\u2013296 (2017).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"28165473"}]}},{"Citation":"Punjani A, Zhang H &amp; Fleet DJ Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214\u20131221 (2020).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"33257830"}]}},{"Citation":"Pettersen EF et al. UCSF chimera\u2014a visualization system for exploratory research and analysis. J. Comput. Chem 25, 1605\u20131612 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15264254"}]}},{"Citation":"Pettersen EF et al. UCSF ChimeraX: structure visualization for researchers, educators, and developers. Protein Sci. 30, 70\u201382 (2021).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC7737788"},{"@attributes":{"IdType":"pubmed"},"@text":"32881101"}]}},{"Citation":"Jumper J et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583\u2013589 (2021).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC8371605"},{"@attributes":{"IdType":"pubmed"},"@text":"34265844"}]}},{"Citation":"Emsley P &amp; Cowtan K Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126\u20132132 (2004).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15572765"}]}},{"Citation":"Afonine PV et al. Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Crystallogr. D 74, 531\u2013544 (2018).","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC6096492"},{"@attributes":{"IdType":"pubmed"},"@text":"29872004"}]}}]}]}}}