1EFN

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

1EFN の概要

• エントリーDOI: 10.2210/pdb1efn/pdb
• 分子名称: FYN TYROSINE KINASE, HIV-1 NEF PROTEIN, TRIMETHYL LEAD ION, ... (4 entities in total)
• 機能のキーワード: 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)
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane: P06241; Host cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P03406
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49427.04

構造登録者

Lee, C.-H.,Kuriyan, J. (登録日: 1996-06-29, 公開日: 1997-01-11, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)