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首页> 外文期刊>FEBS Letters >Characterisation of the F‐actin binding domains of villin: classification of F‐actin binding proteins into two groups according to their binding sites on actin
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Characterisation of the F‐actin binding domains of villin: classification of F‐actin binding proteins into two groups according to their binding sites on actin

机译:villin F-肌动蛋白结合域的表征:根据F-肌动蛋白结合蛋白在肌动蛋白上的结合位点将其分为两组

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摘要

>The F-actin binding properties of chicken villin, its headpiece and domains 2–3 (V2-3) have been analysed to identify sites involved in bundle formation. Headpiece and V2-3 bind actin with K d values of ~7 μM and ~0.3 μM, respectively, at low ionic strength. V2-3 binding, like that of villin, is weakened with increasing salt concentration; headpiece binding is not. Competition experiments show that headpiece and V2-3 bind to different sites on actin, forming the two cross-linking sites of villin. Headpiece does not compete with the F-actin binding domains of gelsolin or α-actinin, but it dissociates actin depolymerizing factor. We suggest that the F-actin binding domains of actin severing, crosslinking and capping proteins can be organized into two classes.
机译:>已分析了鸡villin,其头部和结构域2-3(V2-3)的F-肌动蛋白结合特性,以鉴定参与束形成的位点。在低离子强度下,Headpiece和V2-3结合肌动蛋白的 K d 值分别约为〜7μM和〜0.3μM。 V2-3的结合与villin的结合一样,随着盐浓度的增加而减弱。耳机绑定不是。竞争实验表明,头饰和V2-3与肌动蛋白上的不同位点结合,形成了villin的两个交联位点。头饰不与凝溶胶蛋白或α-肌动蛋白的F-肌动蛋白结合域竞争,但它解离了肌动蛋白解聚因子。我们建议肌动蛋白切断,交联和封盖蛋白的F-肌动蛋白结合域可以组织为两类。

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