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The human immunodeficiency virus (HIV-1) infects T lymphocytes via an interaction between the virus envelope glycoprotein gp120 and the CD4 antigen of T helper cells. Previous studies demonstrated that mutations in various regions of CD4 domain 1 lead to the loss of gp120 binding. In the present study the gp120 binding site was constructed in rat CD4 by replacing rat with human CD4 sequence. A series of mutants was constructed the best of which bound gp120 with an affinity only twofold less than that of human CD4. The data indicate that the gp120 binding site of human CD4 is constituted by residues 33-58 of domain 1.

Type

Journal article

Journal

J Exp Med

Publication Date

01/01/1992

Volume

175

Pages

301 - 304

Keywords

Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antigens, CD4, Binding Sites, Binding Sites, Antibody, HIV Envelope Protein gp120, HIV-1, Models, Structural, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, Rats, Sequence Homology, Nucleic Acid