{"PubmedArticle":{"MedlineCitation":{"@attributes":{"Status":"MEDLINE","Owner":"NLM","IndexingMethod":"Manual"},"PMID":{"@attributes":{"Version":"1"},"@text":"27396829"},"DateCompleted":{"Year":"2017","Month":"10","Day":"05"},"DateRevised":{"Year":"2020","Month":"12","Day":"09"},"Article":{"@attributes":{"PubModel":"Print-Electronic"},"Journal":{"ISSN":{"@attributes":{"IssnType":"Electronic"},"@text":"1878-4186"},"JournalIssue":{"@attributes":{"CitedMedium":"Internet"},"Volume":"24","Issue":"8","PubDate":{"Year":"2016","Month":"Aug","Day":"02"}},"Title":"Structure (London, England : 1993)","ISOAbbreviation":"Structure"},"ArticleTitle":"Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding.","Pagination":{"StartPage":"1372","EndPage":"1379","MedlinePgn":"1372-1379"},"ELocationID":[{"@attributes":{"EIdType":"doi","ValidYN":"Y"},"@text":"10.1016\/j.str.2016.05.013"},{"@attributes":{"EIdType":"pii","ValidYN":"Y"},"@text":"S0969-2126(16)30119-8"}],"Abstract":{"AbstractText":["The Gastrulation Brain Homeobox 1 (Gbx1) gene encodes the Gbx1 homeodomain that targets TAATTA motifs in double-stranded DNA (dsDNA). Residues Glu17 and Arg52 in Gbx1 form a salt bridge, which is preserved in crystal structures and molecular dynamics simulations of homologous homeodomain-DNA complexes. In contrast, our nuclear magnetic resonance (NMR) studies show that DNA binding to Gbx1 induces dynamic local polymorphisms, which include breaking of the Glu17-Arg52 salt bridge. To study this interaction, we produced a variant with Glu17Arg and Arg52Glu mutations, which exhibited the same fold as the wild-type protein, but a 2-fold reduction in affinity for dsDNA. Analysis of the NMR structures of the Gbx1 homeodomain in the free form, the Gbx1[E17R,R52E] variant, and a Gbx1 homeodomain-DNA complex showed that stabilizing interactions of the Arg52 side chain with the DNA backbone are facilitated by transient breakage of the Glu17-Arg52 salt bridge in the DNA-bound Gbx1."],"CopyrightInformation":"Copyright \u00a9 2016 Elsevier Ltd. All rights reserved."},"AuthorList":{"@attributes":{"CompleteYN":"Y"},"Author":[{"@attributes":{"ValidYN":"Y"},"LastName":"Proudfoot","ForeName":"Andrew","Initials":"A","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Joint Center for Structural Genomics, La Jolla, CA 92037, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Geralt","ForeName":"Michael","Initials":"M","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Joint Center for Structural Genomics, La Jolla, CA 92037, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Elsliger","ForeName":"Marc-Andre","Initials":"MA","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Joint Center for Structural Genomics, La Jolla, CA 92037, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Wilson","ForeName":"Ian A","Initials":"IA","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Joint Center for Structural Genomics, La Jolla, CA 92037, USA."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"W\u00fcthrich","ForeName":"Kurt","Initials":"K","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Joint Center for Structural Genomics, La Jolla, CA 92037, USA; Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: wuthrich@scripps.edu."}]},{"@attributes":{"ValidYN":"Y"},"LastName":"Serrano","ForeName":"Pedro","Initials":"P","AffiliationInfo":[{"Affiliation":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: serrano@scripps.edu."}]}]},"Language":["eng"],"GrantList":{"@attributes":{"CompleteYN":"Y"},"Grant":[{"GrantID":"U54 GM094586","Acronym":"GM","Agency":"NIGMS NIH HHS","Country":"United States"}]},"PublicationTypeList":{"PublicationType":[{"@attributes":{"UI":"D016428"},"@text":"Journal Article"}]},"ArticleDate":[{"@attributes":{"DateType":"Electronic"},"Year":"2016","Month":"07","Day":"07"}]},"MedlineJournalInfo":{"Country":"United States","MedlineTA":"Structure","NlmUniqueID":"101087697","ISSNLinking":"0969-2126"},"ChemicalList":{"Chemical":[{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"C422443"},"@text":"GBX1 protein, human"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D018398"},"@text":"Homeodomain Proteins"}},{"RegistryNumber":"0","NameOfSubstance":{"@attributes":{"UI":"D011994"},"@text":"Recombinant Proteins"}},{"RegistryNumber":"9007-49-2","NameOfSubstance":{"@attributes":{"UI":"D004247"},"@text":"DNA"}}]},"CitationSubset":["IM"],"MeshHeadingList":{"MeshHeading":[{"DescriptorName":{"@attributes":{"UI":"D000595","MajorTopicYN":"N"},"@text":"Amino Acid Sequence"}},{"DescriptorName":{"@attributes":{"UI":"D019943","MajorTopicYN":"Y"},"@text":"Amino Acid Substitution"}},{"DescriptorName":{"@attributes":{"UI":"D001665","MajorTopicYN":"N"},"@text":"Binding Sites"}},{"DescriptorName":{"@attributes":{"UI":"D003001","MajorTopicYN":"N"},"@text":"Cloning, Molecular"}},{"DescriptorName":{"@attributes":{"UI":"D004247","MajorTopicYN":"N"},"@text":"DNA"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"Y"},"@text":"chemistry"},{"@attributes":{"UI":"Q000235","MajorTopicYN":"N"},"@text":"genetics"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"}]},{"DescriptorName":{"@attributes":{"UI":"D004926","MajorTopicYN":"N"},"@text":"Escherichia coli"},"QualifierName":[{"@attributes":{"UI":"Q000235","MajorTopicYN":"N"},"@text":"genetics"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"}]},{"DescriptorName":{"@attributes":{"UI":"D015870","MajorTopicYN":"N"},"@text":"Gene Expression"}},{"DescriptorName":{"@attributes":{"UI":"D018398","MajorTopicYN":"N"},"@text":"Homeodomain Proteins"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"Y"},"@text":"chemistry"},{"@attributes":{"UI":"Q000235","MajorTopicYN":"N"},"@text":"genetics"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"}]},{"DescriptorName":{"@attributes":{"UI":"D006801","MajorTopicYN":"N"},"@text":"Humans"}},{"DescriptorName":{"@attributes":{"UI":"D062105","MajorTopicYN":"N"},"@text":"Molecular Docking Simulation"}},{"DescriptorName":{"@attributes":{"UI":"D056004","MajorTopicYN":"N"},"@text":"Molecular Dynamics Simulation"}},{"DescriptorName":{"@attributes":{"UI":"D009154","MajorTopicYN":"N"},"@text":"Mutation"}},{"DescriptorName":{"@attributes":{"UI":"D019906","MajorTopicYN":"N"},"@text":"Nuclear Magnetic Resonance, Biomolecular"}},{"DescriptorName":{"@attributes":{"UI":"D011485","MajorTopicYN":"N"},"@text":"Protein Binding"}},{"DescriptorName":{"@attributes":{"UI":"D000072756","MajorTopicYN":"N"},"@text":"Protein Conformation, alpha-Helical"}},{"DescriptorName":{"@attributes":{"UI":"D000072757","MajorTopicYN":"N"},"@text":"Protein Conformation, beta-Strand"}},{"DescriptorName":{"@attributes":{"UI":"D054730","MajorTopicYN":"N"},"@text":"Protein Interaction Domains and Motifs"}},{"DescriptorName":{"@attributes":{"UI":"D011994","MajorTopicYN":"N"},"@text":"Recombinant Proteins"},"QualifierName":[{"@attributes":{"UI":"Q000737","MajorTopicYN":"N"},"@text":"chemistry"},{"@attributes":{"UI":"Q000235","MajorTopicYN":"N"},"@text":"genetics"},{"@attributes":{"UI":"Q000378","MajorTopicYN":"N"},"@text":"metabolism"}]},{"DescriptorName":{"@attributes":{"UI":"D016415","MajorTopicYN":"N"},"@text":"Sequence Alignment"}},{"DescriptorName":{"@attributes":{"UI":"D013816","MajorTopicYN":"N"},"@text":"Thermodynamics"}}]},"KeywordList":[{"@attributes":{"Owner":"NOTNLM"},"Keyword":[{"@attributes":{"MajorTopicYN":"N"},"@text":"Binding affinity"},{"@attributes":{"MajorTopicYN":"N"},"@text":"J-UNIO"},{"@attributes":{"MajorTopicYN":"N"},"@text":"NMR structure determination"},{"@attributes":{"MajorTopicYN":"N"},"@text":"protein:DNA complex"}]}]},"PubmedData":{"History":{"PubMedPubDate":[{"@attributes":{"PubStatus":"received"},"Year":"2016","Month":"1","Day":"19"},{"@attributes":{"PubStatus":"revised"},"Year":"2016","Month":"3","Day":"30"},{"@attributes":{"PubStatus":"accepted"},"Year":"2016","Month":"5","Day":"6"},{"@attributes":{"PubStatus":"entrez"},"Year":"2016","Month":"7","Day":"12","Hour":"6","Minute":"0"},{"@attributes":{"PubStatus":"pubmed"},"Year":"2016","Month":"7","Day":"12","Hour":"6","Minute":"0"},{"@attributes":{"PubStatus":"medline"},"Year":"2017","Month":"10","Day":"6","Hour":"6","Minute":"0"},{"@attributes":{"PubStatus":"pmc-release"},"Year":"2016","Month":"11","Day":"15"}]},"PublicationStatus":"ppublish","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"27396829"},{"@attributes":{"IdType":"mid"},"@text":"NIHMS827800"},{"@attributes":{"IdType":"pmc"},"@text":"PMC5109927"},{"@attributes":{"IdType":"doi"},"@text":"10.1016\/j.str.2016.05.013"},{"@attributes":{"IdType":"pii"},"@text":"S0969-2126(16)30119-8"}]},"ReferenceList":[{"Reference":[{"Citation":"Babin V, Wang D, Rose RB, Sagui C. Binding polymorphism in the DNA bound state of the Pdx1 homeodomain. Plos Comput Biol. 2013;9:e1003160.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3738460"},{"@attributes":{"IdType":"pubmed"},"@text":"23950697"}]}},{"Citation":"Baird-Titus JM, Clark-Baldwin K, Dave V, Caperelli CC, Ma J, Rance M. The solution structure of the native K50 Bicoid homeodomain bound to the consensus TAATCC DNA-binding site. J Mol Biol. 2006;356:1137\u20131151.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"16406070"}]}},{"Citation":"Banerjee-Basu S, Baxevanis AD. Molecular evolution of the homeodomain family of transcription factor. Nucleic Acids Res. 2001;29:3258\u20133269.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC55828"},{"@attributes":{"IdType":"pubmed"},"@text":"11470884"}]}},{"Citation":"Bartels C, Xia TH, Billeter M, G\u00fcntert P, W\u00fcthrich K. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J Biomol NMR. 1995;6:1\u201310.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"22911575"}]}},{"Citation":"Billeter M, Qian Y, Otting G, M\u00fcller M, Gehring W, W\u00fcthrich K. Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy. J Mol Biol. 1990;214:183\u2013197.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"2164583"}]}},{"Citation":"Billeter M, Qian Y, Otting G, M\u00fcller M, Gehring W, W\u00fcthrich K. Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J Mol Biol. 1993;234:1084\u20131094.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"7903398"}]}},{"Citation":"Billeter M, G\u00fcntert P, Luginb\u00fchl P, W\u00fcthrich K. Hydration and DNA recognition by homeodomains. Cell. 1996;85:1057\u20131065.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8674112"}]}},{"Citation":"Buckley DM, Burroughs-Garcia J, Lewandoski M, Waters ST. Characterization of the Gbx1 \u2212\/\u2212 mouse mutant: A requirement for Gbx1 in normal locomotion and sensorimotor circuit development. Plos One. 2013;8:e56214.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3572027"},{"@attributes":{"IdType":"pubmed"},"@text":"23418536"}]}},{"Citation":"Chaney BA, Clark-Baldwin K, Dave V, Ma J, Rance M. Solution structure of the K50 class homeodomain PITX2 bound to DNA and implications for mutations that cause Rieger syndrome. Biochemistry. 2005;44:7497\u20137511.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"15895993"}]}},{"Citation":"Clarke ND. Covariation of residues in the homeodomain sequence family. Prot Sci. 1995;4:2269\u20132278.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2143025"},{"@attributes":{"IdType":"pubmed"},"@text":"8563623"}]}},{"Citation":"Cleaver JE. Profile of Tomas Lindhal, Paul Modrich, and Aziz Sancar, 2015 Nobel laureates in chemistry. Proc Natl Acad Sci USA. 2016;113:242\u2013245.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4720345"},{"@attributes":{"IdType":"pubmed"},"@text":"26715755"}]}},{"Citation":"Chi YI. Homeodomain revisited: a lesson from disease-causing mutations. Hum Genet. 2005;116:433\u2013444.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1579204"},{"@attributes":{"IdType":"pubmed"},"@text":"15726414"}]}},{"Citation":"Cornell WD, Cieplak P, Bayly CI, Gould IR, Merz KM, Ferguson DM, et al. A 2nd generation force-field for the simulation of proteins, nucleic-acids and organic-molecules. J Am Chem Soc. 1995;117:5179\u201397."},{"Citation":"Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WWB, III, Snoeyink J, Richardson JS, Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucl Acid Res. 2007;35:W375\u2013W383.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1933162"},{"@attributes":{"IdType":"pubmed"},"@text":"17452350"}]}},{"Citation":"De Vries SJ, van Dijk ADJ, Krzeminski M, van Dijk M, Thureau A, Hsu V, et al. HADDOCK versus HADDOCK: New features and performance of HADDOCK2.0 on the CAPRI targets. Proteins: Struct Funct Bioinf. 2007;69:726\u2013733.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"17803234"}]}},{"Citation":"Dominguez C, Boelens R, Bonvin AMJJ. HADDOCK: A protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc. 2003;125:1731\u20131737.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12580598"}]}},{"Citation":"Flader W, Wellenzohn B, Winger RH, Hallbrucker A, Mayer E, Liedl KR. Stepwise induced fit in the pico- to nanosecond time scale governs the complexation of the even-skipped transcriptional repressor homeodomain to DNA. Biopolymers. 2003;68:139\u2013149.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12548619"}]}},{"Citation":"Fiorito F, Herrmann T, Damberger FF, W\u00fcthrich K. Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D 1H,1H-NOESY. Journal of Biomolecular NMR. 2008;42:23\u201333.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"18709333"}]}},{"Citation":"Grant RA, Rould MA, Klemm JD, Pabo CO. Exploring the role of glutamine 50 in the homeodomain-DNA interface: Crystal structure of engrailed (Gln50 -&gt; Ala) complex at 2.0 angstrom. Biochemistry. 2000;39:8187\u20138192.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"10889025"}]}},{"Citation":"G\u00fcntert P, Mumenthaler C, W\u00fcthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997;273:283\u2013298.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"9367762"}]}},{"Citation":"Herrmann T, G\u00fcntert P, W\u00fcthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR. 2002;24:171\u2013189.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12522306"}]}},{"Citation":"Herrmann T, G\u00fcntert P, W\u00fcthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002;319:209\u2013227.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12051947"}]}},{"Citation":"Hiller S, Fiorito F, W\u00fcthrich K, Wider G. Automated projection spectroscopy (APSY) Proc Natl Acad Sci USA. 2005;102:10876\u201310881.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1182451"},{"@attributes":{"IdType":"pubmed"},"@text":"16043707"}]}},{"Citation":"Hiller S, Wider G, W\u00fcthrich K. APSY-NMR with proteins: practical aspects and backbone assignment. J Biomol NMR. 2008;42:179\u2013195.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"18841481"}]}},{"Citation":"Hovde S, Abate-Shen C, Geiger JH. Crystal structure of the Msx-1 homeodomain\/DNA complex. Biochemistry. 2001;40:12013\u201312021.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"11580277"}]}},{"Citation":"Jauch R, Ng CKL, Saikatendu KS, Stevens RG, Kolatkar PR. Crystal structure and DNA binding of the homeodomain of the stem cell transcription factor Nanog. J Mol Biol. 2008;376:758\u2013770.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"18177668"}]}},{"Citation":"John A, Wildner H, Britsch S. The homeodomain transcription factor Gbx1 identifies a subpopulation of late-born GABAergic interneurons in the developing dorsal spinal cord, Dev. Dyn. 2005;234:767\u2013771.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"16193514"}]}},{"Citation":"Koradi R, Billeter M, W\u00fcthrich K. MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph. 1996;14:51\u201355.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8744573"}]}},{"Citation":"Koradi R, Billeter M, Guntert P. Point-centered domain decomposition for parallel molecular dynamics simulation. Comput Phys Commun. 2000;124:139\u201347."},{"Citation":"Lindahl T. My journey to DNA repair. Gen Prot Bioninf. 2013;11:2\u20137.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC4357663"},{"@attributes":{"IdType":"pubmed"},"@text":"23453014"}]}},{"Citation":"Longo A, Guanga GP, Rose RB. Structural basis for induced fit mechanisms in DNA recognition by the Pdx1 homeodomain. Biochemistry. 2007;46:2948\u20132957.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"17315980"}]}},{"Citation":"Luginb\u00fchl P, G\u00fcntert P, Billeter M, W\u00fcthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR. 1996;8:136\u2013146.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8914272"}]}},{"Citation":"Meziane H, Fraulob V, Riet F, Krezel W, Selloum M, Geffarth M, et al. The homeodomain factor Gbx1 is required for locomotion and cell specification in the dorsal spinal cord. PeerJ. 2013;1:e142.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3757465"},{"@attributes":{"IdType":"pubmed"},"@text":"24010020"}]}},{"Citation":"Modrich P. Mechanisms in eukariotic mismatch repair. J Biol Chem. 2006;281:30305\u201330309.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2234602"},{"@attributes":{"IdType":"pubmed"},"@text":"16905530"}]}},{"Citation":"Otting G, Qian Y, Billeter M, M\u00fcller M, Affolter M, Gehring W, et al. Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 1990;9:3085\u20133092.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC552035"},{"@attributes":{"IdType":"pubmed"},"@text":"1976507"}]}},{"Citation":"Qian Y, Billeter M, Otting G, M\u00fcller M, Gehring W, W\u00fcthirch K. The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors. Cell. 1989;61:573\u2013780.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"2572329"}]}},{"Citation":"Rhinn M, Lun K, Werner M, Simeone A, Brand M. Isolation and expression of the homeobox gene Gbx1 during mouse development. Dev Dyn. 2004;229:334\u2013339.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"14745958"}]}},{"Citation":"Sancar A. DNA excision repair. Annu Rev Biochem. 1996;65:43\u201381.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8811174"}]}},{"Citation":"Serrano P, Pedrini B, Mohanty B, Geralt M, Herrmann T, W\u00fcthrich K. The J-UNIO protocol for automated protein structure determination by NMR in solution. J Biomol NMR. 2012;53:341\u2013354.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3541938"},{"@attributes":{"IdType":"pubmed"},"@text":"22752932"}]}},{"Citation":"Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, Li W, et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol. 2011;7:539.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC3261699"},{"@attributes":{"IdType":"pubmed"},"@text":"21988835"}]}},{"Citation":"Torrado M, Revuelta J, Gonzalez C, Corzana F, Bastida A, Asensio JL. Role of conserved salt bridges in homeodomain stability and DNA binding. J Biol Chem. 2009;284:23765\u201323779.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2749150"},{"@attributes":{"IdType":"pubmed"},"@text":"19561080"}]}},{"Citation":"van Dijk M, van Dijk ADJ, Hsu V, Boelens R, Bonvin AMJJ. Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility. Nucleic Acids Res. 2006;34:3317\u20133325.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC1500871"},{"@attributes":{"IdType":"pubmed"},"@text":"16820531"}]}},{"Citation":"van Dijk M, Bonvin AMJJ. 3D-DART: a DNA structure modelling server. Nucleic Acids Res. 2009;37:W235\u2013W239.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pmc"},"@text":"PMC2703913"},{"@attributes":{"IdType":"pubmed"},"@text":"19417072"}]}},{"Citation":"Volk J, Herrmann T, W\u00fcthrich K. Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH. Journal of Biomolecular NMR. 2008;41:127\u201338.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"18512031"}]}},{"Citation":"Waters ST, Wilson CP, Lewandoski M. Cloning and embryonic expression analysis of the mouse Gbx1 gene, Gene Expr. Patterns. 2003;3:313\u2013317.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"12799077"}]}},{"Citation":"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, et al. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. Journal of Biomolecular NMR. 1995;6:135\u201340.","ArticleIdList":{"ArticleId":[{"@attributes":{"IdType":"pubmed"},"@text":"8589602"}]}},{"Citation":"W\u00fcthrich K. NMR of Proteins and Nucleic Acids. New York: Wiley; 1996."},{"Citation":"Zwahlen C, Legault P, Vincent SJF, Greenblatt J, Konrat R, Kay LE. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage lambda N-peptide\/boxB RNA complex. J Am Chem Soc. 1997;119:6711\u2013672."}]}]}}}