Sprang S R
Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas 75235-9050, USA.
Curr Opin Struct Biol. 1997 Dec;7(6):849-56. doi: 10.1016/s0959-440x(97)80157-1.
G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.
G蛋白来自一个多样的调节性GTP酶家族,在结合GTP的状态下,它们与下游效应器结合并激活效应器。与效应器结构域结合的Ras同源物的结构揭示了G蛋白将GTP结合与效应器激活偶联并实现特异性的机制。结构不相关的GTP酶激活蛋白与互补G蛋白之间的复合物表明,通过与G蛋白构象不稳定的开关区域直接相互作用来刺激GTP水解的共同机制。