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 Bioljournal_title
Journal of molecular biologyauthors
Dayhoff JE,Shoemaker BA,Bryant SH,Panchenko ARdoi
10.1016/j.jmb.2009.10.052subject
Has Abstractpub_date
2010-01-29 00:00:00pages
860-70issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(09)01311-4journal_volume
395pub_type
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pub_type: 杂志文章
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更新日期:2010-01-29 00:00:00
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更新日期:1994-02-18 00:00:00
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更新日期:2007-10-05 00:00:00
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更新日期:2004-01-02 00:00:00
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更新日期:1991-10-05 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of molecular biology
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更新日期:2006-02-17 00:00:00
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更新日期:2015-06-19 00:00:00
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pub_type: 杂志文章
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更新日期:2008-07-18 00:00:00
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
pub_type: 杂志文章
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更新日期:2005-02-11 00:00:00