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Titolo:
Characterization and molecular basis of the oligomeric structure of HIV-1 Nef protein
Autore:
Arold, S; Hoh, F; Domergue, S; Birck, C; Delsuc, MA; Jullien, M; Dumas, C;
Indirizzi:
Univ Montpellier 1, U414 INSERM, UMR C5048 CNRS, Ctr Biochim Struct, F-34060 Montpellier, France Univ Montpellier 1 Montpellier France F-34060 -34060 Montpellier, France CNRS, IPBS, Grp Cristallog Biol, F-31077 Toulouse, France CNRS Toulouse France F-31077 p Cristallog Biol, F-31077 Toulouse, France
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 6, volume: 9, anno: 2000,
pagine: 1137 - 1148
SICI:
0961-8368(200006)9:6<1137:CAMBOT>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; CD4 DOWN-REGULATION; LONG-TERM SURVIVOR; SH3 DOMAIN; VIRAL INFECTIVITY; LIGHT-SCATTERING; DILEUCINE MOTIF; BINDING SURFACE; PHYSICAL INTERACTION; DIMERIC ASSOCIATION;
Keywords:
chemical cross-linking; dynamic light scattering; HIV-1; Nef; NMR; oligomerization; sedimentation equilibrium;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
83
Recensione:
Indirizzi per estratti:
Indirizzo: Dumas, C Univ Montpellier 1, U414 INSERM, UMR C5048 CNRS, Ctr Biochim Struct, 15 Ave C Flahault, F-34060 Montpellier, France Univ Montpellier 1 15 Ave C Flahault Montpellier France F-34060
Citazione:
S. Arold et al., "Characterization and molecular basis of the oligomeric structure of HIV-1 Nef protein", PROTEIN SCI, 9(6), 2000, pp. 1137-1148

Abstract

The Nef protein of human immunodeficiency virus type I (HIV-1) is an important determinant for the onset of AIDS disease. The self-association properties of HIV-1 Nef are analyzed by chemical cross-linking, dynamic light scattering, equilibrium analytical ultracentrifugation, and NMR spectroscopy. The experimental data show that the HN-I Nef core domain forms stable homo-dimers and trimers in solution, but not higher oligomers. These Nef homomers are not covalently linked by disulfide bridges, and the equilibrium between these forms is dependent on the Nef concentration. We further provide the molecular basis for the Nef core dimers and trimers obtained by analysis of crystallographic models. Oligomerization of biological polypeptides is acommon tool used to trigger events in cellular signaling and endocytosis, both of which an targeted by Nef. The quaternary structure of Nef may be ofphysiological importance and may help to connect its cellular targets or to increase affinity of the viral molecule for its ligands. The herein described models for Nef dimers and trimers will allow further mutational studies to elucidate their role in vivo. These results provide novel insight intothe structural and functional relationships of this important viral protein. Moreover, the oligomer intel face may represent a novel target for the design of antiviral agents.

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Documento generato il 04/12/20 alle ore 20:08:35