结晶态的丝切蛋白-β-肌动蛋白的结构。
The structure of crystalline profilin-beta-actin.
作者信息
Schutt C E, Myslik J C, Rozycki M D, Goonesekere N C, Lindberg U
机构信息
Department of Chemistry, Henry H. Hoyt Laboratory, Princeton University, New Jersey 08544.
出版信息
Nature. 1993 Oct 28;365(6449):810-6. doi: 10.1038/365810a0.
The three-dimensional structure of bovine profilin-beta-actin has been solved to 2.55 A resolution by X-ray crystallography. There are several significant local changes in the structure of beta-actin compared with alpha-actin as well as an overall 5 degrees rotation between its two major domains. Actin molecules in the crystal are organized into ribbons through intermolecular contacts like those found in oligomeric protein assemblies. Profilin forms two extensive contacts with the actin ribbon, one of which appears to correspond to the solution contact in vitro.
通过X射线晶体学，已将牛源肌动蛋白结合蛋白-β-肌动蛋白的三维结构解析到2.55埃的分辨率。与α-肌动蛋白相比，β-肌动蛋白的结构存在几个显著的局部变化，并且其两个主要结构域之间整体旋转了5度。晶体中的肌动蛋白分子通过分子间接触组织成条带，类似于在寡聚蛋白组装体中发现的那些接触。肌动蛋白结合蛋白与肌动蛋白条带形成两个广泛的接触，其中一个似乎对应于体外溶液中的接触。
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