1EFN

HIV-1 NEF PROTEIN IN COMPLEX WITH R96I MUTANT FYN SH3 DOMAIN

Summary for 1EFN

• Entry DOI: 10.2210/pdb1efn/pdb
• Descriptor: FYN TYROSINE KINASE, HIV-1 NEF PROTEIN, TRIMETHYL LEAD ION, ... (4 entities in total)
• Functional Keywords: complex (sh3 domain-viral enhancer), proto-oncogene, transferase, tyrosine-protein kinase, phosphorylation, aids, myristylation, gtp-binding, atp-binding, sh3 domain, sh2 domain, ppii helix, pxxp motif, complex (sh3 domain-viral enhancer) complex, complex (sh3 domain/viral enhancer)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane: P06241; Host cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P03406
• Total number of polymer chains: 4
• Total formula weight: 49427.04

Authors

Lee, C.-H.,Kuriyan, J. (deposition date: 1996-06-29, release date: 1997-01-11, Last modification date: 2024-02-07)

Primary citation

Lee, C.H.,Saksela, K.,Mirza, U.A.,Chait, B.T.,Kuriyan, J.
Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
Cell(Cambridge,Mass.), 85:931-942, 1996

PubMed 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.

PubMed: 8681387
DOI: 10.1016/S0092-8674(00)81276-3

Experimental method

X-RAY DIFFRACTION (2.5 Å)