title: Docking of peptide-T onto the D1 domain of the CD4 receptor.
abstract: Peptide T (pepT) is a segment of the human immunodeficiency virus (HIV) envelope protein gp120. The peptide competitively binds to the CD4 receptor of a subset of peripheral T lymphocytes and inhibits binding of gp120. Previous studies of this laboratory allowed the assessment of a bioactive form of the peptide and a pharmacophore for the peptide-receptor interaction. In the present study the proposed bioactive form of pepT and its (4-8) segment, the smallest pepT fragment shown to retain full activity, were docked onto the D1 domain of the CD4 receptor. The bioactive conformation of the peptides complements well a cleft on the surface of the CD4 receptor, shown to be the attachment site of gp120 from site directed mutagenesis experiments. These studies provide an improved description of the ligand-receptor pharmacophore.
authors.affiliation: Dept. d'Enginyeria Quimica, UPC; ETS d'Enginyers Industrials, Barcelona, Spain. juanje@eq.upc.es
authors.forename: J J
authors.initials: JJ
authors.lastname: Perez
authors.forename: M
authors.initials: M
authors.lastname: Filizola
authors.forename: F
authors.initials: F
authors.lastname: Corcho
mesh_terms: D000678:Amygdalin / Q000378:metabolism; D015704:CD4 Antigens / Q000737:chemistry / Q000378:metabolism*; D003198:Computer Simulation; D015195:Drug Design; D008024:Ligands; D008958:Models, Molecular; D015717:Peptide T / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D015704:CD4 Antigens; D008024:Ligands; D015717:Peptide T; D000678:Amygdalin