STRUCTURE OF GELSOLIN SEGMENT-1-ACTIN COMPLEX AND THE MECHANISM OF FILAMENT SEVERING
STRUCTURE OF GELSOLIN SEGMENT-1-ACTIN COMPLEX AND THE MECHANISM OF FILAMENT SEVERING
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DOI：
10.1038/364685a0
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发表时间：
1993-08-19
期刊：
影响因子：
64.8
通讯作者：
WEEDS, AG
中科院分区：
文献类型：
--
作者：
MCLAUGHLIN, PJ;GOOCH, JT;WEEDS, AG
凝溶胶蛋白是一种在细胞中使肌动蛋白丝断裂的蛋白质，其第1结构域与肌动蛋白形成复合物的结构已被报道。第1结构域利用肌动蛋白结构域之间裂隙中由氢键环绕的非极性斑块结合单体。在肌动蛋白丝模型上，它相切结合，仅破坏一条螺旋链中相邻亚基之间的那些接触。第1结构域的折叠方式对于凝溶胶蛋白家族的所有结构域是通用的，因为保守残基形成了该结构的核心。它也为理解由一种凝溶胶蛋白变体引起的淀粉样变性的起源提供了基础。
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.