The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1
The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1
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DOI：
10.1016/s1097-2765(00)80389-5
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发表时间：
1999-11-01
期刊：
影响因子：
16
通讯作者：
Hakoshima, T
中科院分区：
文献类型：
--
作者：
Maesaki, R;Ihara, K;Hakoshima, T
小G蛋白Rho已经成为涉及细胞骨架重组的细胞事件的关键调节因子。在这里，我们报道了与蛋白激酶PKN/PRK1的效应结构域结合的RhoA的2.2埃晶体结构。该结构揭示了效应域的反平行螺旋线圈指(ACC指)折叠，该折叠主要通过特定的氢键与包含开关I、β链B2和B3以及C末端α螺旋A5的Rho特异性决定区结合。ACC指折与其他小G蛋白不同，为效应器识别的不同方式提供了证据。基于结构的序列分析表明，ACC指折在Rho效应器蛋白中广泛存在。
The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 Angstrom crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.