Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
Cell
; 85(6): 931-42, 1996 Jun 14.
Article
em En
| MEDLINE
| ID: mdl-8681387
ABSTRACT
The crystal structure of the conserved core of HIV-1 Nef has been determined in complex with the SH3 domain of a mutant Fyn tyrosine kinase (a single amino acid substitution, Arg-96 to isoleucine), to which Nef binds tightly. The conserved PxxP sequence motif of Nef, known to be important for optimal viral replication, is part of a polyproline type II helix that engages the SH3 domain in a manner resembling closely the interaction of isolated peptides with SH3 domains. The Nef-SH3 structure also reveals how high affinity and specificity in the SH3 interaction is achieved by the presentation of the PxxP motif within the context of the folded structure of Nef.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Tirosina Quinases
/
Produtos do Gene nef
/
Proteínas Proto-Oncogênicas
/
HIV-1
/
Domínios de Homologia de src
Limite:
Humans
Idioma:
En
Revista:
Cell
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Estados Unidos