Normal-mode analysis suggests important flexibility between the two N-terminal domains of CD4 and supports the hypothesis of a conformational change in CD4 upon HIV binding

Protein Engineering

Volumn 9, Issue 8, 1996, Pages 671-677

  Sanejouand, Y H ^a  

^a CNRS   (France)

Author keywords

gp120; HIV blocking monoclonal antibodies; Human immunodeficiency virus; Second domain of CD4; Virus entry

Indexed keywords

CD4 ANTIGEN; ENVELOPE PROTEIN; GLYCOPROTEIN GP 120; VIRUS RECEPTOR;

AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; VIRUS INFECTIVITY;

HUMAN IMMUNODEFICIENCY VIRUS;

EID: 0029791008     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.8.671     Document Type: Article

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