1. RODNA
  2. CONICET
  3. CONICET
Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.creatorJack, Benjamin R.-
dc.creatorMeyer, Austin G.-
dc.creatorEchave, Julián-
dc.creatorWilke, Claus O.-
dc.date2018-05-11T21:26:11Z-
dc.date2018-05-11T21:26:11Z-
dc.date2016-05-
dc.date2018-05-11T20:38:19Z-
dc.date.accessioned2019-04-29T15:50:24Z-
dc.date.available2019-04-29T15:50:24Z-
dc.date.issued2016-05-
dc.identifierJack, Benjamin R.; Meyer, Austin G.; Echave, Julián; Wilke, Claus O.; Functional Sites Induce Long-Range Evolutionary Constraints in Enzymes; Public Library of Science; PLoS Biology; 14; 5; 5-2016; 1-23; e1002452-
dc.identifierhttp://hdl.handle.net/11336/45007-
dc.identifier1545-7885-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/303407-
dc.descriptionFunctional residues in proteins tend to be highly conserved over evolutionary time. However, to what extent functional sites impose evolutionary constraints on nearby or even more distant residues is not known. Here, we report pervasive conservation gradients toward catalytic residues in a dataset of 524 distinct enzymes: evolutionary conservation decreases approximately linearly with increasing distance to the nearest catalytic residue in the protein structure. This trend encompasses, on average, 80% of the residues in any enzyme, and it is independent of known structural constraints on protein evolution such as residue packing or solvent accessibility. Further, the trend exists in both monomeric and multimeric enzymes and irrespective of enzyme size and/or location of the active site in the enzyme structure. By contrast, sites in protein–protein interfaces, unlike catalytic residues, are only weakly conserved and induce only minor rate gradients. In aggregate, these observations show that functional sites, and in particular catalytic residues, induce long-range evolutionary constraints in enzymes.-
dc.descriptionFil: Jack, Benjamin R.. University of Texas at Austin; Estados Unidos-
dc.descriptionFil: Meyer, Austin G.. University of Texas at Austin; Estados Unidos-
dc.descriptionFil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos-
dc.formatapplication/pdf-
dc.formatapplication/zip-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherPublic Library of Science-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1371/journal.pbio.1002452-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.1002452-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectProtein-
dc.subjectEvolution-
dc.subjectFunctional-
dc.subjectConstraints-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.subjectOtras Ciencias Químicas-
dc.subjectCiencias Químicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleFunctional Sites Induce Long-Range Evolutionary Constraints in Enzymes-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro sencillo del ítem