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Titolo:
ANALYSIS OF THE SECONDARY STRUCTURE OF THE CATALYTIC DOMAIN OF MOUSE RAS EXCHANGE FACTOR CDC25(MM)
Autore:
COCCETTI P; MONZANI E; ALBERGHINA L; CASELLA L; MARTEGANI E;
Indirizzi:
UNIV MILAN,DIPARTIMENTO FISIOL & BIOCHIM GEN,SEZ BIOCHIM COMPARATA,VIA CELORIA 26 I-20133 MILAN ITALY UNIV MILAN,DIPARTIMENTO FISIOL & BIOCHIM GEN,SEZ BIOCHIM COMPARATA I-20133 MILAN ITALY UNIV PAVIA,DIPARTIMENTO CHIM GEN I-27100 PAVIA ITALY UNIV MILAN,FAC SCI MF NAT 3 I-21100 VARESE ITALY
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 2, volume: 1383, anno: 1998,
pagine: 292 - 300
SICI:
0167-4838(1998)1383:2<292:AOTSSO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE-RELEASING FACTOR; PROTEIN-MEDIATED SIGNALS; BETA-GAMMA-SUBUNITS; SACCHAROMYCES-CEREVISIAE; MOLECULAR MECHANISM; CIRCULAR-DICHROISM; KINETIC-PROPERTIES; CLONING; BRAIN; IDENTIFICATION;
Keywords:
GDP/GTP EXCHANGE FACTOR; RAS PROTEIN; P21 RAS-GEF INTERACTION; BACTERIAL EXPRESSION; PROTEIN PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
P. Coccetti et al., "ANALYSIS OF THE SECONDARY STRUCTURE OF THE CATALYTIC DOMAIN OF MOUSE RAS EXCHANGE FACTOR CDC25(MM)", Biochimica et biophysica acta. Protein structure and molecular enzymology, 1383(2), 1998, pp. 292-300

Abstract

The minimal active domain (GEF domain) of the mouse Ras exchange factor CDC25(Mm) was purified to homogeneity from recombinant Escherichia coli culture. The 256 amino acids polypeptide shows high activity in vitro and forms a stable complex with H-ras p21 in absence of guanine nucleotides. Circular dichroism (CD) spectra in the far UV region indicate that this domain is highly structured with a high content of alpha-helix (42%). Near UV CD spectra evidenced good signal due to phenylalanine and tyrosine while a poor contribution was elicited by the threetryptophan residues contained in this domain. The tryptophan fluorescence signal was scarcely affected by denaturation of the protein or byformation of the binary complex with H-ras p21, suggesting that the Trp residues, which are well conserved in the GEF domain of several Ras-exchange factors, were exposed to the surface of the protein and theyare not most probably directly involved in the interaction with Ras proteins. (C) 1998 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 10:39:00