Crystal structure of the GABAA-receptor-associated protein, GABARAP
Crystal structure of the GABAA-receptor-associated protein, GABARAP
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DOI：
10.1093/embo-reports/kvf026
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发表时间：
2002-02-01
期刊：
影响因子：
7.7
通讯作者：
Weissenhorn, W
中科院分区：
文献类型：
--
作者：
Bavro, VN;Sola, M;Weissenhorn, W
GABA(A)受体相关蛋白(GABARAP)是细胞内膜转运和/或融合蛋白家族中的一员，参与了GABA(A)受体的质膜靶向和/或再循环。GABARAP定位于细胞内膜，如跨高尔基网络，与GABAA受体的72个亚基结合，并与微管和N-乙基马来酰亚胺敏感因子相互作用。我们报道了哺乳动物GABARAP在2.0埃分辨率下的X射线晶体结构。GABARAP由一个与微管蛋白结合有关的N末端基本螺旋区和一个具有保守的泛素样折叠的核心结构组成。与从植物到哺乳动物的GABARAP同源物之间高度保守的序列一致，核心结构的一个面绝对保守，而相反的面显示出相当大的差异。这些特征与该家族所有成员共享的保守的表面介导蛋白质-蛋白质相互作用相一致，而非保守的表面区可能发挥特定的作用，如与特定的膜受体对接。
The GABA(A)-receptor-associated protein (GABARAP) is a member of a growing family of intracellular membrane trafficking and/or fusion proteins and has been implicated in plasma membrane targeting and/or recycling of GABA(A) receptors. GABARAP is localized on intracellular membranes such as the trans-Golgi network, binds to the 72 subunit of GABAA receptors and interacts with microtubules and the N-ethylmaleimide-sensitive factor. We report the X-ray crystal structure of mammalian GABARAP at 2.0 Angstrom resolution. GABARAP consists of an N-terminal basic helical region, which has been implicated in tubulin binding, and a core structure with a conserved ubiquitin-like fold. Consistent with the high extent of sequence conservation among GABARAP homologues from plants to mammals, one face of the core structure is absolutely conserved while the opposite face shows considerable divergence. These features are in agreement with the conserved surface mediating protein-protein interactions shared by all members of the family, whereas the non-conserved surface region may play specific roles, such as docking to particular membrane receptors.