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dc.contributor.authorRodriguez-Rivas, Juan
dc.contributor.authorMarsili, Simone
dc.contributor.authorJuan, David
dc.contributor.authorValencia, Alfonso 
dc.date.accessioned2019-07-10T09:32:58Z
dc.date.available2019-07-10T09:32:58Z
dc.date.issued2016
dc.identifier.citationProc Natl Acad Sci U S A. 2016;113(52):15018-15023es_ES
dc.identifier.issn0027-8424es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/7879
dc.description.abstractProtein-protein interactions are fundamental for the proper functioning of the cell. As a result, protein interaction surfaces are subject to strong evolutionary constraints. Recent developments have shown that residue coevolution provides accurate predictions of heterodimeric protein interfaces from sequence information. So far these approaches have been limited to the analysis of families of prokaryotic complexes for which large multiple sequence alignments of homologous sequences can be compiled. We explore the hypothesis that coevolution points to structurally conserved contacts at protein-protein interfaces, which can be reliably projected to homologous complexes with distantly related sequences. We introduce a domain-centered protocol to study the interplay between residue coevolution and structural conservation of protein-protein interfaces. We show that sequence-based coevolutionary analysis systematically identifies residue contacts at prokaryotic interfaces that are structurally conserved at the interface of their eukaryotic counterparts. In turn, this allows the prediction of conserved contacts at eukaryotic protein-protein interfaces with high confidence using solely mutational patterns extracted from prokaryotic genomes. Even in the context of high divergence in sequence (the twilight zone), where standard homology modeling of protein complexes is unreliable, our approach provides sequence-based accurate information about specific details of protein interactions at the residue level. Selected examples of the application of prokaryotic coevolutionary analysis to the prediction of eukaryotic interfaces further illustrate the potential of this approach.es_ES
dc.description.sponsorshipWe thank F. Abascal and M. L. Tress for helpful discussions. This work was supported by Spanish Ministry of Economy and Competitiveness Projects BFU2015-71241-R and BIO2012-40205, cofunded by the European Regional Development Fund.es_ES
dc.language.isoenges_ES
dc.publisherNATL ACAD SCIENCESes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectcoevolutiones_ES
dc.subjectcontact predictiones_ES
dc.subjecthomology modelinges_ES
dc.subjectprotein complexes_ES
dc.subjectprotein–protein interactiones_ES
dc.subject.meshBiological Evolution es_ES
dc.subject.meshCatalytic Domain es_ES
dc.subject.meshComputational Biology es_ES
dc.subject.meshDatabases, Proteines_ES
dc.subject.meshEukaryota es_ES
dc.subject.meshHumans es_ES
dc.subject.meshModels, Statisticales_ES
dc.subject.meshProkaryotic Cells es_ES
dc.subject.meshProtein Binding es_ES
dc.subject.meshProtein Interaction Mapping es_ES
dc.subject.meshProtein Multimerization es_ES
dc.subject.meshProteins es_ES
dc.subject.meshReproducibility of Results es_ES
dc.subject.meshSequence Alignment es_ES
dc.subject.meshSequence Homology es_ES
dc.subject.meshEvolution, Moleculares_ES
dc.subject.meshMutation es_ES
dc.titleConservation of coevolving protein interfaces bridges prokaryote-eukaryote homologies in the twilight zonees_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID27965389es_ES
dc.format.volume113es_ES
dc.format.number52es_ES
dc.format.page15018-15023es_ES
dc.identifier.doi10.1073/pnas.1611861114es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderEuropean Regional Development Fund (ERDF/FEDER)es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1091-6490es_ES
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.1611861114.es_ES
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaes_ES
dc.repisalud.institucionCNIOes_ES
dc.repisalud.orgCNIOCNIO::Grupos de investigación::Grupo de Biología Computacional Estructurales_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU2015-71241-Res_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BIO2012-40205es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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