Phosphorylation in protein-protein binding: Effect on stability and function

Hafumi Nishi, Kosuke Hashimoto, Anna R. Panchenko

研究成果: Article査読

166 被引用数 (Scopus)

抄録

Posttranslational modifications offer a dynamic way to regulate protein activity, subcellular localization, and stability. Here we estimate the effect of phosphorylation on protein binding and function for different types of complexes from human proteome. We find that phosphorylation sites tend to be located on binding interfaces in heterooligomeric and weak transient homooligomeric complexes. Analysis of molecular mechanisms of phosphorylation shows that phosphorylation may modulate the strength of interactions directly on interfaces and that binding hotspots tend to be phosphorylated in heterooligomers. Although the majority of complexes do not show significant estimated stability differences upon phosphorylation or dephosphorylation, for about one-third of all complexes it causes relatively large changes in binding energy. We discuss the cases where phosphorylation mediates the complex formation and regulates the function. We show that phosphorylation sites are more likely to be evolutionary conserved than other interfacial residues.

本文言語English
ページ(範囲)1807-1815
ページ数9
ジャーナルStructure
19
12
DOI
出版ステータスPublished - 2011 12 7
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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