Docking of peptide-T onto the D1 domain of the CD4 receptor

J Biomol Struct Dyn. 2000 Feb;17(4):725-33. doi: 10.1080/07391102.2000.10506562.


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.

MeSH terms

  • Amygdalin / metabolism
  • CD4 Antigens / chemistry
  • CD4 Antigens / metabolism*
  • Computer Simulation
  • Drug Design
  • Ligands
  • Models, Molecular
  • Peptide T / metabolism*
  • Protein Binding
  • Protein Structure, Tertiary*


  • CD4 Antigens
  • Ligands
  • Peptide T
  • Amygdalin