STRUCTURE OF GELSOLIN SEGMENT-1-ACTIN COMPLEX AND THE MECHANISM OF FILAMENT SEVERING

被引：524

作者：

MCLAUGHLIN, PJ ^{[1
]}

GOOCH, JT ^{[1
]}

MANNHERZ, HG ^{[1
]}

WEEDS, AG ^{[1
]}

机构：

[1] UNIV MARBURG,INST CYTOBIOL & CYTOPATHOL,W-3550 MARBURG,GERMANY

来源：

NATURE | 1993年 / 364卷 / 6439期

关键词：

D O I：

10.1038/364685a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.

引用

页码：685 / 692

页数：8

共 46 条

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