Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
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DOI：
10.1016/s0092-8674(00)80836-3
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发表时间：
2000-04-28
期刊：
影响因子：
64.5
通讯作者：
Karplus, PA
中科院分区：
文献类型：
--
作者：
Pearson, MA;Reczek, D;Karplus, PA
ezrin-radixin-moesin （ERM）蛋白家族通过c端F-actin结合片段和n端FERM结构域（一种常见的膜结合模块）将细胞表面结构的肌动蛋白丝连接到质膜上。ERM蛋白受FERM和c端尾部结构域的分子内结合调控，这掩盖了它们的结合位点。休眠moesin FERM/tail复合物的晶体结构表明，FERM结构域具有三个紧凑的裂片，包括一个集成的PTB/PH/ EVH1折叠，c端段结合为一个扩展肽，覆盖了FERM结构域的大表面。这种扩展的结合模式为不同的信号如何产生不同程度的激活提供了一种新的机制。序列保守表明肿瘤抑制基因merlin也有类似的调控。
The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites. The crystal structure of a dormant moesin FERM/tail complex reveals that the FERM domain has three compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal segment bound as an extended peptide masking a large surface of the FERM domain. This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin.