Crystal structure of human V-1 in the apo form
Crystal structure of human V-1 in the apo form
复制标题
apo 形式的人 V-1 的晶体结构
DOI：
10.1107/s2053230x20016829
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发表时间：
2021
期刊：
影响因子：
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通讯作者：
Motonori Ota
中科院分区：
文献类型：
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作者：
Shuichi Takeda;Ryotaro Koike;Takayuki Nagae;Ikuko Fujiwara;Akihiro Narita;Yuichiro Maeda;Motonori Ota
V-1，也称为肌营养蛋白，是一种13 kDa的锚定重复序列蛋白，其结合并抑制异二聚体肌动蛋白帽蛋白（CP），其是细胞骨架肌动蛋白动力学的关键调节因子。 与CP复合的V-1的晶体结构显示，V-1通过跨越几个锚蛋白重复的残基识别CP。在此，在不存在特异性配体的情况下以2.3 μ m分辨率报告了人V-1的晶体结构。 在不对称单元中，晶体包含两个具有几乎相同结构的V-1单体（Cα r.m.s.d.）。0.47分）。 两条apo V-1链的整体结构也与CP结合V-1的结构高度相似（Cα r.m.s.d.s <0.50 μ m），表明CP不会诱导V-1发生较大的构象变化。 使用计算程序All Atom Motion Tree的详细结构比较显示，CP结合可以通过几个残基的轻微侧链重排来完成。这些发现与V-1的已知生物学作用一致，其中V-1全面抑制细胞质中的CP。
V-1, also known as myotrophin, is a 13 kDa ankyrin-repeat protein that binds and inhibits the heterodimeric actin capping protein (CP), which is a key regulator of cytoskeletal actin dynamics. The crystal structure of V-1 in complex with CP revealed that V-1 recognizes CP via residues spanning several ankyrin repeats. Here, the crystal structure of human V-1 is reported in the absence of the specific ligand at 2.3 Å resolution. In the asymmetric unit, the crystal contains two V-1 monomers that exhibit nearly identical structures (Cα r.m.s.d. of 0.47 Å). The overall structures of the two apo V-1 chains are also highly similar to that of CP-bound V-1 (Cα r.m.s.d.s of <0.50 Å), indicating that CP does not induce a large conformational change in V-1. Detailed structural comparisons using the computational program All Atom Motion Tree revealed that CP binding can be accomplished by minor side-chain rearrangements of several residues. These findings are consistent with the known biological role of V-1, in which it globally inhibits CP in the cytoplasm.