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首页> 外文期刊>Cell motility and the cytoskeleton >Villin-type headpiece domains show a wide range of F-actin-binding affinities.
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Villin-type headpiece domains show a wide range of F-actin-binding affinities.

机译：维尔林型头盔域显示了广泛的F-肌动蛋白结合亲和力。

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摘要

The villin-type "headpiece" domain is a modular motif found at the extreme C-terminus of larger "core" domains in over 25 cytoskeletal proteins in plants and animals. Although headpiece is classified as an F-actin-binding domain, it has been suggested that some expressed fusion-proteins containing headpiece may lack F-actin-binding in vivo. To determine the intrinsic F-actin affinity of headpiece domains, we quantified the F-actin affinity of seven headpiece domains and three N-terminal truncations, under identical in vitro conditions. The constructs are folded and adopt the native headpiece structure. However, they show a wide range of affinities that can be grouped into high, low, and nonspecific-binding categories. Computer models of the structure and charged surface potential of these headpiece domains suggest features important for high F-actin affinity. We conclude that not all headpiece domains are intrinsically F-actin-binding motifs, and suggest that the surface charge distribution may be an important element for F-actin recognition. Cell Motil. Cytoskeleton 52:9-21, 2002.
机译：villin型“头饰”结构域是在植物和动物的25种以上细胞骨架蛋白中的较大“核心”结构域的极端C末端发现的模块化基序。尽管将头饰分类为F-肌动蛋白结合结构域，但是已经表明，某些包含头饰的表达融合蛋白在体内可能缺乏F-肌动蛋白结合。为了确定耳机域的固有F-肌动蛋白亲和力，我们在相同的体外条件下，对七个耳机域和三个N端截短的F-肌动蛋白亲和力进行了定量。结构被折叠并采用本机头戴式结构。但是，它们显示了广泛的亲和力，可以分为高，低和非特异性结合类别。这些耳机域的结构和带电表面电势的计算机模型表明了对高F-肌动蛋白亲和力很重要的特征。我们得出结论，并不是所有的耳机域本质上都是F-肌动蛋白结合基序，并表明表面电荷分布可能是F-肌动蛋白识别的重要元素。细胞动力。细胞骨架52：9-21，2002。

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