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Titolo:
INTERACTION OF HUMAN RETINAL RGS WITH G-PROTEIN ALPHA-SUBUNITS
Autore:
NATOCHIN M; LIPKIN VM; ARTEMYEV NO;
Indirizzi:
UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS,5-660 BSB IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT PHYSIOL & BIOPHYS IOWA CITY IA 52242 RUSSIAN ACAD SCI,SHEMYAKIN & OVCHINNIKOV INST BIOORGAN CHEM MOSCOW 117871 RUSSIA
Titolo Testata:
FEBS letters
fascicolo: 2-3, volume: 411, anno: 1997,
pagine: 179 - 182
SICI:
0014-5793(1997)411:2-3<179:IOHRRW>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ROD OUTER SEGMENTS; CRYSTAL-STRUCTURE; TRANSDUCIN; GTP; BINDING; MECHANISM; PHOSPHODIESTERASE; BOVINE; SITES; CGMP;
Keywords:
G-PROTEIN; TRANSDUCIN; REGULATOR OF G-PROTEIN SIGNALING; RETINA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
M. Natochin et al., "INTERACTION OF HUMAN RETINAL RGS WITH G-PROTEIN ALPHA-SUBUNITS", FEBS letters, 411(2-3), 1997, pp. 179-182

Abstract

A novel family of RGS proteins negatively regulates signaling via heterotrimeric G-proteins by accelerating the GTPase activity of G-protein alpha subunits. We have investigated interaction of human retinal RGS protein (hRGSr) with in vitro translated G(alpha) subunits: G(t alpha), G(i alpha 1), G(o alpha) and G(s alpha). hRGSr binds well to G(t alpha), G(i alpha 1) and G(o alpha) in the presence of AlF4-, but does not interact with G(s alpha). The N- and C-terminally truncated G(alpha) subunits interact with hRGSr similarly to the intact G(alpha) polypeptides. Analysis of interaction between hRGSr and G(o alpha)/G(s alpha) chimeras suggests that a region of G(o alpha), G(o alpha)22-212, contains major structural determinants for binding to RGS proteins. (C) 1997 Federation of European Biochemical Societies.

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Documento generato il 25/01/21 alle ore 03:26:58