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Titolo:
Structure-function relationships in HIV-1 Nef
Autore:
Geyer, M; Fackler, OT; Peterlin, BM;
Indirizzi:
Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA Univ Heidelberg, Inst Hyg, Dept Virol, D-69120 Heidelberg, Germany Univ Heidelberg Heidelberg Germany D-69120 , D-69120 Heidelberg, Germany
Titolo Testata:
EMBO REPORTS
fascicolo: 7, volume: 2, anno: 2001,
pagine: 580 - 585
SICI:
1469-221X(200107)2:7<580:SRIHN>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; CD4 DOWN-REGULATION; CELL-SURFACE CD4; MUTATIONAL ANALYSIS; HUMAN THIOESTERASE; CRYSTAL-STRUCTURE; DILEUCINE MOTIF; RHESUS MACAQUES; SH3 DOMAINS; BETA-COP;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Geyer, M Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 CA 94143 USA
Citazione:
M. Geyer et al., "Structure-function relationships in HIV-1 Nef", EMBO REP, 2(7), 2001, pp. 580-585

Abstract

The accessory Nef protein of HIV and SIV is essential for viral pathogenesis, yet it is perplexing in its multitude of molecular functions. In this review we analyse the structure-function relationships of motifs recently proposed to play roles in aspects of Nef modification, signalling and trafficking, and thereby to impinge on the ability of the virus to survive in, andto manipulate, its cellular host. Based on the full-length structure assembly of HIV Nef, we correlate surface accessibility with secondary structureelements and sequence conservation. Motifs involved in Nef-mediated CD4 and MHC I downregulation are located in flexible regions of Nef, suggesting that the formation of the transient trafficking complexes involved in these processes depends on the recognition of primary sequences. In contrast, theinteraction sites for signalling molecules that contain SH3 domains or thep21-activated kinases are associated with the well folded core domain, suggesting the recognition of highly structured protein surfaces.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:19:11