The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation

Leslie D. Burtnick, Edward K. Koepf, Jonathan Grimes, E. Yvonne Jones, David I. Stuart, Paul J. McLaughlin, Robert C. Robinson

研究成果査読

247 被引用数 (Scopus)

抄録

The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. We propose that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. Domain shifts are proposed in response to Ca2+ as bases for models of how gelsolin acts to sever, cap, or nucleate F-actin filaments. The structure also invites discussion of polyphosphoinositide binding to segment 2 and suggests how mutation at Asp- 187 could initiate a series of events that lead to deposition of amyloid plaques, as observed in victims of familial amyloidosis (Finnish type).

本文言語English
ページ(範囲)661-670
ページ数10
ジャーナルCell
90
4
DOI
出版ステータスPublished - 8月 22 1997
外部発表はい

ASJC Scopus subject areas

  • 生化学、遺伝学、分子生物学一般

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