Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A
Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany.
Nature. 1995 Jun 15;375(6532):554-60. doi: 10.1038/375554a0.
The X-ray crystal structure of the complex between the Ras-related protein Rap1A in the GTP-analogue (GppNHp) form and the Ras-binding domain (RBD) of the Ras effector molecule c-Raf1, a Ser/Thr-specific protein kinase, has been solved to a resolution of 2.2 A. It shows that RBD 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 RBD 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.
已解析出处于GTP类似物（GppNHp）形式的Ras相关蛋白Rap1A与Ras效应分子c-Raf1（一种丝氨酸/苏氨酸特异性蛋白激酶）的Ras结合结构域（RBD）之间复合物的X射线晶体结构，分辨率达到2.2埃。结果表明，RBD具有泛素超折叠结构，且Rap1A的结构与Ras的结构非常相似。两种蛋白之间的相互作用由RBD的B1 - B2链和Rap1A的β2 - β3链形成的明显中央反平行β折叠介导。复合物的形成由Rap1A开关I区域中所谓效应子残基的主链和侧链相互作用介导。
