title: CD4-gp120 interactions.
abstract: The three-dimensional structure of the binding domain of the CD4 molecule has been determined and extensive mutational analyses of the respective binding sites on gp120 and CD4 have been completed. The consequences of gp120-CD4 binding with respect to secondary changes in the virion, or the cell, that may be required for infection or that may interfere with cellular function are current active areas of investigation.
authors.affiliation: Centers for Disease Control, Atlanta, Georgia.
authors.forename: J S
authors.initials: JS
authors.lastname: McDougal
authors.forename: D R
authors.initials: DR
authors.lastname: Klatzmann
authors.forename: P J
authors.initials: PJ
authors.lastname: Maddon
mesh_terms: D000163:Acquired Immunodeficiency Syndrome / Q000276:immunology; D000595:Amino Acid Sequence; D000937:Antigen-Antibody Reactions; D015704:CD4 Antigens / Q000235:genetics / Q000276:immunology*; D015496:CD4-Positive T-Lymphocytes / Q000276:immunology; D000939:Epitopes / Q000235:genetics; D015699:HIV Envelope Protein gp120 / Q000235:genetics / Q000276:immunology*; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure
chemical_list: D015704:CD4 Antigens; D000939:Epitopes; D015699:HIV Envelope Protein gp120