Miura K, Kamiya H, Kubota S, Ikehara M, Nishimura S, Ohtsuka E
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Protein Eng. 1988 Sep;2(3):227-31. doi: 10.1093/protein/2.3.227.
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.
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。
