Intrinsic disorder accelerates dissociation rather than association

Koji Umezawa, Jun Ohnuki, Junichi Higo, Mitsunori Takano*

*この研究の対応する著者

研究成果: Article査読

20 被引用数 (Scopus)

抄録

The intrinsically disordered protein (IDP) has distinct properties both physically and biologically: it often becomes folded when binding to the target and is frequently involved in signal transduction. The physical property seems to be compatible with the biological property where fast association and dissociation between IDP and the target are required. While fast association has been well studied, fueled by the fly-casting mechanism, the dissociation kinetics has received less attention. We here study how the intrinsic disorder affects the dissociation kinetics, as well as the association kinetics, paying attention to the interaction strength at the binding site (i.e., the quality of the “fly lure”). Coarse-grained molecular dynamics simulation of the pKID-KIX system, a well-studied IDP system, shows that the association rate becomes larger as the disorder-inducing flexibility that was imparted to the model is increased, but the acceleration is marginal and turns into deceleration as the quality of the fly lure is worsened. In contrast, the dissociation rate is greatly enhanced as the disorder is increased, indicating that intrinsic disorder serves for rapid signal switching more effectively through dissociation than association. Proteins 2016; 84:1124–1133.

本文言語English
ページ(範囲)1124-1133
ページ数10
ジャーナルProteins: Structure, Function and Bioinformatics
84
8
DOI
出版ステータスPublished - 2016 8 1

ASJC Scopus subject areas

  • 構造生物学
  • 生化学
  • 分子生物学

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