| GeneLibs

题目:: Structure-based design, synthesis, and activity of peptide inhibitors of RGS4 GAP activity.
作者:: Jin(Yafei),Zhong(Huailing),Omnaas(John R),Neubig(Richard R),Mosberg(Henry I)
状态:: 发布时间2004-08-17 , 更新时间 2013-11-21
期刊:: Methods Enzymol
摘要:: One of the principal roles of the multifunctional regulator of G-protein signaling (RGS) proteins is to terminate G-protein-coupled receptor (GPCR) signaling by binding to the G-protein Galpha subunit, thus acting as GTPase-activating proteins (GAPs). In principle, then, selective inhibitors of this GAP function would have potential as therapeutic agents, as they could be used to augment the effects of endogenous or exogenous GPCR agonists. Using the published RGS4-G(ialpha1) X-ray structure, we have designed and synthesized a series of cyclic peptides, modeled on the G(ialpha) switch I region, that inhibit RGS4 GAP activity, presumably by blocking the interaction between RGS4 and G(ialpha1). These compounds should prove useful for elucidating RGS-mediated activity and serve as a starting point for the development of a novel class of therapeutic agent.
语言:: eng
DOI:

文献库文献相关信息