Structure-based design, synthesis, and pharmacologic evaluation of peptide RGS4 inhibitors

Autor:	Y, Jin, H, Zhong, J R, Omnaas, R R, Neubig, H I, Mosberg
Rok vydání:	2004
Předmět:	Inhibitory Concentration 50 Structure-Activity Relationship Cricetulus Cricetinae GTPase-Activating Proteins Animals CHO Cells Peptides Cyclic RGS Proteins
Zdroj:	The journal of peptide research : official journal of the American Peptide Society. 63(2)
ISSN:	1397-002X
Popis:	Regulators of G-protein signaling (RGS) proteins form a multifunctional signaling family. A key role of RGS proteins is binding to the G-protein Galpha-subunit and acting as GTPase-activating proteins (GAPs), thereby rapidly terminating G protein-coupled receptor (GPCR) signaling. Using the published RGS4-Gialpha1 X-ray structure we have designed and synthesized a series of cyclic peptides, modeled on the Gialpha Switch I region, that inhibit RGS4 GAP activity. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::61d10f1ba5d583022acf391f763a1ec9 https://pubmed.ncbi.nlm.nih.gov/15009535 Zobrazit plný text záznamu Plný text