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埃兹蛋白FERM结构域的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of the ezrin FERM domain.

作者信息

Smith William J, Cerione Richard A

机构信息

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1359-61. doi: 10.1107/s0907444902010004. Epub 2002 Jul 20.

Abstract

Ezrin is a member of the ERM (ezrin/radixin/moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and that also function, both upstream and downstream of the small G-protein Rho, in signaling cascades that regulate the assembly of actin stress fibers. In this study, crystals were obtained of the amino-terminal 297 residues (referred to as FERM) of ezrin. The crystals of the FERM domain of ezrin belong to the monoclinic space group P2(1), with unit-cell parameters a = 48.5, b = 112.8, c = 66.3 A, beta = 102.3 degrees, and contain two molecules in the asymmetric unit. A 2.3 A data set was collected using synchrotron radiation at CHESS A1.

摘要

埃兹蛋白是ERM(埃兹蛋白/根蛋白/膜突蛋白)家族的一员,该家族蛋白将肌动蛋白细胞骨架与质膜交联起来,并且在小G蛋白Rho的上下游发挥作用,参与调节肌动蛋白应激纤维组装的信号级联反应。在本研究中,获得了埃兹蛋白氨基端297个残基(称为FERM)的晶体。埃兹蛋白FERM结构域的晶体属于单斜空间群P2(1),晶胞参数为a = 48.5、b = 112.8、c = 66.3 Å,β = 102.3°,不对称单元中含有两个分子。使用CHESS A1的同步辐射收集了分辨率为2.3 Å的数据集。

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