Evolution of protein binding modes in homooligomers.

Abstract:

:The evolution of protein interactions cannot be deciphered without a detailed analysis of interaction interfaces and binding modes. We performed a large-scale study of protein homooligomers in terms of their symmetry, interface sizes, and conservation of binding modes. We also focused specifically on the evolution of protein binding modes from nine families of homooligomers and mapped 60 different binding modes and oligomerization states onto the phylogenetic trees of these families. We observed a significant tendency for the same binding modes to be clustered together and conserved within clades on phylogenetic trees; this trend is especially pronounced for close homologs with 70% sequence identity or higher. Some binding modes are conserved among very distant homologs, pointing to their ancient evolutionary origin, while others are very specific for a certain phylogenetic group. Moreover, we found that the most ancient binding modes have a tendency to involve symmetrical (isologous) homodimer binding arrangements with larger interfaces, while recently evolved binding modes more often exhibit asymmetrical arrangements and smaller interfaces.

journal_name

J Mol Biol

authors

Dayhoff JE,Shoemaker BA,Bryant SH,Panchenko AR

doi

10.1016/j.jmb.2009.10.052

subject

Has Abstract

pub_date

2010-01-29 00:00:00

pages

860-70

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)01311-4

journal_volume

395

pub_type

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