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Titolo:
HIV-1 NEF PROTEIN - PURIFICATION, CRYSTALLIZATIONS, AND PRELIMINARY-X-RAY DIFFRACTION STUDIES
Autore:
FRANKEN P; AROLD S; PADILLA A; BODEUS M; HOH F; STRUB MP; BOYER M; JULLIEN M; BENAROUS R; DUMAS C;
Indirizzi:
UNIV MONTPELLIER 1,CTR BIOCHIM STRUCT,UMR C9955 CNRS,U414 INSERM,FAC PHARM,15 AVE C FLAHAULT F-34060 MONTPELLIER FRANCE UNIV MONTPELLIER 1,CTR BIOCHIM STRUCT,UMR C9955 CNRS,U414 INSERM,FAC PHARM F-34060 MONTPELLIER FRANCE INST COCHIN GENET MOL,INSERM U332 F-75014 PARIS FRANCE
Titolo Testata:
Protein science
fascicolo: 12, volume: 6, anno: 1997,
pagine: 2681 - 2683
SICI:
0961-8368(1997)6:12<2681:HNP-PC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYNAMIC LIGHT-SCATTERING; SH3 DOMAIN; KINASES;
Keywords:
CRYSTALLIZATION; HIV-1; NEF; SH3 DOMAIN; SRC KINASE FAMILY;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
12
Recensione:
Indirizzi per estratti:
Citazione:
P. Franken et al., "HIV-1 NEF PROTEIN - PURIFICATION, CRYSTALLIZATIONS, AND PRELIMINARY-X-RAY DIFFRACTION STUDIES", Protein science, 6(12), 1997, pp. 2681-2683

Abstract

Human immunodeficiency virus Nef protein accelerates virulent progression of AIDS by its interaction with specific cellular proteins involved in cellular activation and signal transduction. Here we report the purification and crystallization of the conserved core of HN-1(LAI) Nef protein in the unliganded form and in complex with the wild-type SH3domain of the p59(fyn) protein-tyrosine kinase. One-dimensional NMR experiments show that full-length protein and truncated fragment corresponding to the product of HIV-1 protease cleavage have a well-folded compact tertiary structure. The ligand-free HIV 1 Nef(core) protein forms cubic crystals belonging to space group P23 with unit cell dimensions of a = b = c = 86.4 Angstrom. The Nef-Fyn SH3 cocrystals belong to the space group P6(1)22 or its enantiomorph, P6(5)22, with unit cell dimensions of a = b = 108.2 Angstrom and c = 223.7 Angstrom. Both crystal forms diffract to a resolution limit of 3.0 Angstrom resolution using synchrotron radiation, and are thus suitable for X-ray structure determination.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:28:38