Inhibition of regulator of G protein signaling function by two mutant RGS4 proteins

Kirk M. Druey; John H. Kehrl

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Inhibition of regulator of G protein signaling function by two mutant RGS4 proteins

机译：两种突变的RGS4蛋白抑制G蛋白信号传导功能的调节剂

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Regulators of G protein signaling (RGS) proteins limit the lifetime of activated (GTP-bound) hetero- trimeric G protein subunits by acting as GTPase-activating proteins (GAPs). Mutation of two residues in RGS4, which, based on the crystal structure of RGS4 complexed with G_iα1-GDP-AlF_4~-, directly contact G_iα1 (N88 and L159), essen- tially abolished RGS4 binding and GAP activity. Mutation of another contact residue (S164) partially inhibited both bind- ing and GAP activity. Two other mutations, one of a contact residue (R167M/A) and the other an adjacent residue (F168A), also significantly reduced RGS4 binding to G_iα1-GDP-AlF_4~-, but in addition redirected RGS4 binding toward the GTPγS- bound form.

机译：G蛋白信号转导（RGS）蛋白的调节剂通过充当GTPase激活蛋白（GAP）来限制激活的（结合GTP的）异源三聚G蛋白亚基的寿命。基于与G_iα1-GDP-AlF_4〜-复合的RGS4的晶体结构，RGS4中的两个残基突变直接接触G_iα1（N88和L159），基本上消除了RGS4的结合和GAP活性。另一个接触残基的突变（S164）部分抑制了结合和GAP活性。其他两个突变，一个接触残基（R167M / A）和另一个相邻残基（F168A），也显着降低了RGS4与G_iα1-GDP-AlF_4〜-的结合，但另外将RGS4结合重定向到了与GTPγS-结合的形式。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1997年第24期|p.12851-12856|共6页
作者
Kirk M. Druey; John H. Kehrl;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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Inhibition of regulator of G protein signaling function by two mutant RGS4 proteins

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