Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 9, 2014, Pages 3425-3430

  Roche, Julien ^a   Louis, John M ^a   Grishaev, Alexander ^a   Ying, Jinfa ^a   Bax, Adriaan ^a  

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

Author keywords

15N relaxation; Chemical shift; Hemagglutinin; HIV 1 fusion inhibitor; RDC

Indexed keywords

GLYCOPROTEIN GP 41; PHOSPHATIDYLCHOLINE; PHOSPHORYLCHOLINE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; HUMAN IMMUNODEFICIENCY VIRUS 1; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

15N RELAXATION; CHEMICAL SHIFT; HEMAGGLUTININ; HIV-1 FUSION INHIBITOR; RDC;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; GENE COMPONENTS; HIV ENVELOPE PROTEIN GP41; LIPID BILAYERS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; VIRUS INTERNALIZATION; WATER;

EID: 84895806775     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1401397111     Document Type: Article

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