ras蛋白鸟嘌呤核苷酸结合位点的转换导致碱基特异性降低。

Conversion of the guanine nucleotide binding sites of ras protein resulting in the reduction of base specificity.

作者信息

Miura K, Kamiya H, Kubota S, Ikehara M, Nishimura S, Ohtsuka E

机构信息

Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

出版信息

Protein Eng. 1988 Sep;2(3):227-31. doi: 10.1093/protein/2.3.227.

DOI:10.1093/protein/2.3.227

PMID:3070545

Abstract

A gene coding for the novel ras protein, p21X, in which the domains of guanine binding and phosphate binding were exchanged, was constructed and expressed in Escherichia coli. The gene product, p21X, showed GTP binding activity, but no GPTase activity. In addition, p21X revealed binding activity toward ATP and CTP. In a competitive binding assay, [3H]GTP binding to p21X was inhibited in the presence of ATP, CTP and UTP, ITP as well as GDP, GTP and dGTP.

摘要

构建了一个编码新型ras蛋白p21X的基因，其中鸟嘌呤结合结构域和磷酸结合结构域进行了交换，并在大肠杆菌中表达。该基因产物p21X具有GTP结合活性，但没有GPTase活性。此外，p21X还显示出对ATP和CTP的结合活性。在竞争性结合试验中，ATP、CTP、UTP、ITP以及GDP、GTP和dGTP的存在会抑制[3H]GTP与p21X的结合。