1AVV

HIV-1 NEF PROTEIN, UNLIGANDED CORE DOMAIN

Summary for 1AVV

• Entry DOI: 10.2210/pdb1avv/pdb
• Descriptor: NEGATIVE FACTOR (1 entity in total)
• Functional Keywords: myristylation, gtp-binding, phosphorylation, hiv-1, nef, virus, pxxp motif
• Biological source: Human immunodeficiency virus 1
• Cellular location: Host cell membrane ; Lipid-anchor ; Cytoplasmic side : P03406
• Total number of polymer chains: 1
• Total formula weight: 17568.72

Authors

Arold, S.,Franken, P.,Dumas, C. (deposition date: 1997-09-21, release date: 1998-03-25, Last modification date: 2024-05-22)

Primary citation

Arold, S.,Franken, P.,Strub, M.P.,Hoh, F.,Benichou, S.,Benarous, R.,Dumas, C.
The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
Structure, 5:1361-1372, 1997

PubMed Abstract: Human immunodeficiency virus (HIV) Nef protein accelerates virulent progression of acquired immunodeficiency syndrome (AIDS) by its interaction with specific cellular proteins involved in signal transduction and host cell activation. Nef has been shown to bind specifically to a subset of the Src family of kinases. The structures of free Nef and Nef bound to Src homology region 3 (SH3) domain are important for the elucidation of how the affinity and specificity for the Src kinase family SH3 domains are achieved, and also for the development of potential drugs and vaccines against AIDS.

PubMed: 9351809
DOI: 10.1016/S0969-2126(97)00286-4

Experimental method

X-RAY DIFFRACTION (3 Å)