NMR structure of an F-actin-binding "headpiece" motif from villin
NMR structure of an F-actin-binding "headpiece" motif from villin
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DOI：
10.1006/jmbi.1999.3321
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发表时间：
1999-12-17
影响因子：
5.6
通讯作者：
McKnight, CJ
中科院分区：
文献类型：
--
作者：
Vardar, D;Buckley, DA;McKnight, CJ
越来越多的f -肌动蛋白结合蛋白家族在C端有一个模块化的f -肌动蛋白结合头结构域。头饰提供了两个f -肌动蛋白结合位点中的一个，这些位点对纤维束至关重要。在这里，我们报告了第一个功能性头饰结构域的结构。鸡绒毛头饰（HP67）的核磁共振结构揭示了两个子结构域共享一个紧密排列的疏水核心。n端亚结构域包含弯曲，旋转和四个残基α -螺旋以及一个埋藏的组氨酸残基，其赋予ph依赖的折叠。c端子结构域由三个α -螺旋组成，其折叠与ph无关。先前与f -肌动蛋白结合有关的两个残基在N和c端亚结构域之间形成了一个埋藏的盐桥。其余鉴定的肌动蛋白结合残基是溶剂暴露和映射到一个独特的f -肌动蛋白结合表面。(C) 1999学术出版社。
A growing family of F-actin-bundling proteins harbors a modular F-actin-binding headpiece domain at the C terminus. Headpiece provides one of the two F-actin-binding sites essential for filament bundling. Here, we report the first structure of a functional headpiece domain. The NMR structure of chicken villin headpiece (HP67) reveals two subdomains that share a tightly packed hydrophobic core. The N-terminal subdomain contains bends, turns, and a four-residue alpha-helix as well as a buried histidine residue that imparts a pH-dependent folding. The C-terminal subdomain is composed of three alpha-helices and its folding is pH-independent. Two residues previously implicated in F-actin-binding form a buried salt-bridge between the N and C-terminal subdomains. The rest of the identified actin-binding residues are solvent-exposed and map onto a unique F-actin-binding surface. (C) 1999 Academic Press.