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Titolo:
CRYSTAL-STRUCTURES OF THE SMALL G-PROTEIN RAP2A IN COMPLEX WITH ITS SUBSTRATE GTP, WITH GDP AND WITH GTP-GAMMA-S
Autore:
CHERFILS J; MENETREY J; LEBRAS G; LEBRAS G; JANOUEIXLEROSEY I; DEGUNZBURG J; GAREL JR; AUZAT I;
Indirizzi:
LAB ENZYMOL & BIOCHIM STRUCT,CNRS,UPR 9063,AVE TERRASSE F-91198 GIF SUR YVETTE FRANCE INST CURIE,INSERM,U248,SECT RECH F-74231 PARIS 05 FRANCE
Titolo Testata:
EMBO journal
fascicolo: 18, volume: 16, anno: 1997,
pagine: 5582 - 5591
SICI:
0261-4189(1997)16:18<5582:COTSGR>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-DIRECTED MUTAGENESIS; HETEROTRIMERIC G-PROTEIN; EFFECTOR REGION; RAS PROTEIN; EF-TU; ESCHERICHIA-COLI; BINDING PROTEINS; CATALYTIC DOMAIN; H-RAS; HYDROLYSIS;
Keywords:
CRYSTAL STRUCTURE; G PROTEINS; GTP HYDROLYSIS; RAP; RAS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
J. Cherfils et al., "CRYSTAL-STRUCTURES OF THE SMALL G-PROTEIN RAP2A IN COMPLEX WITH ITS SUBSTRATE GTP, WITH GDP AND WITH GTP-GAMMA-S", EMBO journal, 16(18), 1997, pp. 5582-5591

Abstract

The small G protein Rap2A has been crystallized in complex with GDP, GTP and GTP gamma S. The Rap2A-GTP complex is the first structure of asmall G protein with its natural ligand GTP. It shows that the hydroxyl group of Tyr32 forms a hydrogen bond with the gamma-phosphate of GTP and with Gly13. This interaction does not exist in the Rap2A-GTP gamma S complex, Tyr32 is conserved in many small G proteins, which probably also form this hydrogen bond with GTP. In addition, Tyr32 is structurally equivalent to a conserved arginine that binds GTP in trimeric G proteins. The actual participation of Tyr32 in GTP hydrolysis is notyet clear, but several possible roles are discussed. The conformational changes between the GDP and GTP complexes are located essentially in the switch I and II regions as described for the related oncoproteinH-Ras. However, the mobile segments vary in length and in the amplitude of movement. This suggests that even though similar regions might be involved in the GDP-GTP cycle of small G proteins, the details of the changes will be different for each G protein and will ensure the specificity of its interaction with a given set of cellular proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 07:00:18