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dc.contributor.author
Teppa, Roxana Elin
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dc.contributor.author
Zea, Diego Javier
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dc.contributor.author
Marino, Cristina Ester
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dc.date.available
2017-11-30T18:43:31Z
dc.date.issued
2017-10
dc.identifier.citation
Teppa, Roxana Elin; Zea, Diego Javier; Marino, Cristina Ester; Protein-protein interactions leave evolutionary footprints: High molecular coevolution at the core of interfaces; John Wiley & Sons Inc; Protein Science; 26; 12; 10-2017; 2438-2444
dc.identifier.issn
0961-8368
dc.identifier.uri
http://hdl.handle.net/11336/29370
dc.description.abstract
Protein-protein interactions are essential to all aspects of life. Specific interactions result from evolutionary pressure at the interacting interfaces of partner proteins. However, evolutionary pressure is not homogeneous within the interface: for instance, each residue does not contribute equally to the binding energy of the complex. To understand functional differences between residues within the interface, we analyzed their properties in the core and rim regions. Here, we characterized protein interfaces with two evolutionary measures, conservation and coevolution, using a comprehensive dataset of 896 protein complexes. These scores can detect different selection pressures at a given position in a multiple sequence alignment. We also analyzed how the number of interactions in which a residue is involved influences those evolutionary signals. We found that the coevolutionary signal is higher in the interface core than in the interface rim region. Additionally, the difference in coevolution between core and rim regions is comparable to the known difference in conservation between those regions. Considering proteins with multiple interactions, we found that conservation and coevolution increase with the number of different interfaces in which a residue is involved, suggesting that more constraints (i.e., a residue that must satisfy a greater number of interactions) allow fewer sequence changes at those positions, resulting in higher conservation and coevolution values. These findings shed light on the evolution of protein interfaces and provide information useful for identifying protein interfaces and predicting protein-protein interactions
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
John Wiley & Sons Inc
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Coevolution
dc.subject
Protein-Protein Interaction
dc.subject
Evolution
dc.subject
Protein Interface
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Protein-protein interactions leave evolutionary footprints: High molecular coevolution at the core of interfaces
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-11-16T15:09:05Z
dc.identifier.eissn
1469-896X
dc.journal.volume
26
dc.journal.number
12
dc.journal.pagination
2438-2444
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
New York
dc.description.fil
Fil: Teppa, Roxana Elin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Zea, Diego Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Marino, Cristina Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.journal.title
Protein Science
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/pro.3318/full
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/pro.3318
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