THE 2.2-ANGSTROM CRYSTAL-STRUCTURE OF THE RAS-BINDING DOMAIN OF THE SERINE THREONINE KINASE C-RAF1 IN COMPLEX WITH RAP1A AND A GTP ANALOG
THE 2.2-ANGSTROM CRYSTAL-STRUCTURE OF THE RAS-BINDING DOMAIN OF THE SERINE THREONINE KINASE C-RAF1 IN COMPLEX WITH RAP1A AND A GTP ANALOG
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DOI：
10.1038/375554a0
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发表时间：
1995-06-15
期刊：
影响因子：
64.8
通讯作者：
WITTINGHOFER, A
中科院分区：
文献类型：
--
作者：
NASSAR, M;HORN, G;WITTINGHOFER, A
Ras相关蛋白Rap 1A的GTP类似物（GppNHp）形式和Ras效应分子c-Raf 1（一种Ser/Thr特异性蛋白激酶）的pas结合结构域（RED）之间的复合物的X射线晶体结构已被解析到2.2埃的分辨率。这表明RED具有泛素超折叠，Rap 1A的结构与Ras非常相似。这两种蛋白质之间的相互作用是由RED的B1-B2链和Rap 1A的β 2-β 3链形成的明显的中央反平行β折叠介导的。复合物的形成是由Rap 1A的开关I区域中所谓的效应残基的主链和侧链相互作用介导的。
The X-ray crystal structure of the complex between the Ras-related protein Rap1A in the GTP-analogue (GppNHp) form and the pas-binding domain (RED) of the Ras effector molecule c-Raf1, a ser/Thr-specific protein kinase, has been solved to a resolution of 2.2 Angstrom. It shows that RED has the ubiquitin superfold and that the structure of Rap1A is very similar to that of Ras. The interaction between the two proteins is mediated by an apparent central antiparallel beta-sheet formed by strands B1-B2 from RED and strands beta 2-beta 3 from Rap1A. Complex formation is mediated by main-chain and side-chain interactions of the so-called effector residues in the switch I region of Rap1A.