The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase

Nature Structural Biology

Volumn 3, Issue 4, 1996, Pages 340-345

  Grzesiek, Stephan ^a   Bax, Ad ^a   Clore, G Marius ^a   Gronenborn, Angela M ^a   Hu, Jin Shan ^a   Kaufman, Joshua ^b   Palmer, Ira ^b   Stahl, Stephen J ^b   Wingfield, Paul T ^b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; NEF PROTEIN; PROTEIN TYROSINE KINASE; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; DRUG DESIGN; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; BINDING SITES; GENE PRODUCTS, NEF; HELIX-TURN-HELIX MOTIFS; HIV-1; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-HCK; SEQUENCE DELETION; SRC HOMOLOGY DOMAINS;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0029881450     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0496-340     Document Type: Article

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