STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE TRIPHOSPHATE CONFORMATION

STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE TRIPHOSPHATE CONFORMATION
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DOI:
10.1038/341209a0
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发表时间:
1989-09-21
期刊:
影响因子:
64.8
通讯作者:
WITTINGHOFER, A
WITTINGHOFER, A
中科院分区:
综合性期刊1区
文献类型:
--
作者:
PAI, EF;KABSCH, W;WITTINGHOFER, A

文献摘要

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p21(氨基酸1-166)与鸟苷三磷酸类似物鸟苷-5′-(β,γ-亚胺)三磷酸(GppNp)络合的鸟嘌呤核苷酸结合域的晶体结构以2.6 Å的分辨率测定。二级结构元素的拓扑顺序与细菌延伸因子EF-Tu的鸟嘌呤核苷酸结合域相同。核苷酸和蛋白质之间的许多相互作用已被确定。讨论了点突变对鸟嘌呤核苷酸结合蛋白氨基酸序列的影响。
The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1–166) complexed to the guanosine triphosphate analogue guanosine-5′-(β,γ-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 Å. 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.