Versatility and invariance in the evolution of homologous heteromeric interfaces.

Evolutionary pressures act on protein complex interfaces so that they preserve their complementarity. Nonetheless, the elementary interactions which compose the interface are highly versatile throughout evolution. Understanding and characterizing interface plasticity across evolution is a fundamenta...

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Autores principales:	Jessica Andreani, Guilhem Faure, Raphaël Guerois
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bcbe69d051bb483f8f20b2e9d3d16461
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spelling	oai:doaj.org-article:bcbe69d051bb483f8f20b2e9d3d164612021-11-18T05:51:03ZVersatility and invariance in the evolution of homologous heteromeric interfaces.1553-734X1553-735810.1371/journal.pcbi.1002677https://doaj.org/article/bcbe69d051bb483f8f20b2e9d3d164612012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22952442/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Evolutionary pressures act on protein complex interfaces so that they preserve their complementarity. Nonetheless, the elementary interactions which compose the interface are highly versatile throughout evolution. Understanding and characterizing interface plasticity across evolution is a fundamental issue which could provide new insights into protein-protein interaction prediction. Using a database of 1,024 couples of close and remote heteromeric structural interologs, we studied protein-protein interactions from a structural and evolutionary point of view. We systematically and quantitatively analyzed the conservation of different types of interface contacts. Our study highlights astonishing plasticity regarding polar contacts at complex interfaces. It also reveals that up to a quarter of the residues switch out of the interface when comparing two homologous complexes. Despite such versatility, we identify two important interface descriptors which correlate with an increased conservation in the evolution of interfaces: apolar patches and contacts surrounding anchor residues. These observations hold true even when restricting the dataset to transiently formed complexes. We show that a combination of six features related either to sequence or to geometric properties of interfaces can be used to rank positions likely to share similar contacts between two interologs. Altogether, our analysis provides important tracks for extracting meaningful information from multiple sequence alignments of conserved binding partners and for discriminating near-native interfaces using evolutionary information.Jessica AndreaniGuilhem FaureRaphaël GueroisPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 8, Iss 8, p e1002677 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Jessica Andreani Guilhem Faure Raphaël Guerois Versatility and invariance in the evolution of homologous heteromeric interfaces.
description	Evolutionary pressures act on protein complex interfaces so that they preserve their complementarity. Nonetheless, the elementary interactions which compose the interface are highly versatile throughout evolution. Understanding and characterizing interface plasticity across evolution is a fundamental issue which could provide new insights into protein-protein interaction prediction. Using a database of 1,024 couples of close and remote heteromeric structural interologs, we studied protein-protein interactions from a structural and evolutionary point of view. We systematically and quantitatively analyzed the conservation of different types of interface contacts. Our study highlights astonishing plasticity regarding polar contacts at complex interfaces. It also reveals that up to a quarter of the residues switch out of the interface when comparing two homologous complexes. Despite such versatility, we identify two important interface descriptors which correlate with an increased conservation in the evolution of interfaces: apolar patches and contacts surrounding anchor residues. These observations hold true even when restricting the dataset to transiently formed complexes. We show that a combination of six features related either to sequence or to geometric properties of interfaces can be used to rank positions likely to share similar contacts between two interologs. Altogether, our analysis provides important tracks for extracting meaningful information from multiple sequence alignments of conserved binding partners and for discriminating near-native interfaces using evolutionary information.
format	article
author	Jessica Andreani Guilhem Faure Raphaël Guerois
author_facet	Jessica Andreani Guilhem Faure Raphaël Guerois
author_sort	Jessica Andreani
title	Versatility and invariance in the evolution of homologous heteromeric interfaces.
title_short	Versatility and invariance in the evolution of homologous heteromeric interfaces.
title_full	Versatility and invariance in the evolution of homologous heteromeric interfaces.
title_fullStr	Versatility and invariance in the evolution of homologous heteromeric interfaces.
title_full_unstemmed	Versatility and invariance in the evolution of homologous heteromeric interfaces.
title_sort	versatility and invariance in the evolution of homologous heteromeric interfaces.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/bcbe69d051bb483f8f20b2e9d3d16461
work_keys_str_mv	AT jessicaandreani versatilityandinvarianceintheevolutionofhomologousheteromericinterfaces AT guilhemfaure versatilityandinvarianceintheevolutionofhomologousheteromericinterfaces AT raphaelguerois versatilityandinvarianceintheevolutionofhomologousheteromericinterfaces
_version_	1718424751594012672

Versatility and invariance in the evolution of homologous heteromeric interfaces.

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