Pai E F, Kabsch W, Krengel U, Holmes K C, John J, Wittinghofer A
Max-Planck-Institut für medizinische Forschung, Abteilung Biophysik, Heidelberg, FRG.
Nature. 1989 Sep 21;341(6239):209-14. doi: 10.1038/341209a0.
The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5'-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. The topological order of secondary structure elements is the same as that of the guanine-nucleotide-binding domain of bacterial elongation factor EF-Tu. Many interactions between nucleotide and protein have been identified. The effects of point mutations and the conservation of amino-acid sequence in the guanine-nucleotide-binding proteins are discussed.
已确定与三磷酸鸟苷类似物鸟苷 - 5'-（β，γ - 亚氨基）三磷酸（GppNp）复合的p21（氨基酸1 - 166）的鸟嘌呤核苷酸结合结构域的晶体结构，分辨率为2.6埃。二级结构元件的拓扑顺序与细菌延伸因子EF - Tu的鸟嘌呤核苷酸结合结构域相同。已确定核苷酸与蛋白质之间的许多相互作用。讨论了点突变的影响以及鸟嘌呤核苷酸结合蛋白中氨基酸序列的保守性。
