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Structure, function, and evolution of transient and obligate protein-protein interactions.

Abstract：

:Recent analyses of high-throughput protein interaction data coupled with large-scale investigations of evolutionary properties of interaction networks have left some unanswered questions. To what extent do protein interactions act as constraints during evolution of the protein sequence? How does the type of interaction, specifically transient or obligate, play into these constraints? Are the mutations in the binding site of an interacting protein correlated with mutations in the binding site of its partner? We address these and other questions by relying on a carefully curated dataset of protein complex structures. Results point to the importance of distinguishing between transient and obligate interactions. We conclude that residues in the interfaces of obligate complexes tend to evolve at a relatively slower rate, allowing them to coevolve with their interacting partners. In contrast, the plasticity inherent in transient interactions leads to an increased rate of substitution for the interface residues and leaves little or no evidence of correlated mutations across the interface.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Mintseris J,Weng Z

doi

10.1073/pnas.0502667102

keywords:

subject

Has Abstract

pub_date

2005-08-02 00:00:00

pages

10930-5

issue

31

eissn

0027-8424

issn

1091-6490

pii

0502667102

journal_volume

102

pub_type

杂志文章

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