Abstract
CD4 glycoprotein on the surface of T cells helps in the immune response and is the receptor for HIV infection. The structure of a soluble fragment of CD4 determined at 2.3 A resolution reveals that the molecule has two intimately associated immunoglobulin-like domains. Residues implicated in HIV recognition by analysis of mutants and antibody binding are salient features in domain D1. Domain D2 is distinguished by a variation on the beta-strand topologies of antibody domains and by an intra-sheet disulphide bridge.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Antibodies, Monoclonal / immunology
-
Binding Sites
-
Biological Evolution
-
CD4 Antigens / ultrastructure*
-
Computer Graphics
-
Crystallography
-
DNA Mutational Analysis
-
HIV Envelope Protein gp120 / metabolism*
-
HLA-D Antigens / metabolism
-
Membrane Fusion
-
Models, Molecular
-
Molecular Sequence Data
-
Molecular Structure
-
Peptide Fragments
-
Protein Conformation
-
Recombinant Proteins
-
Structure-Activity Relationship
-
X-Ray Diffraction
Substances
-
Antibodies, Monoclonal
-
CD4 Antigens
-
HIV Envelope Protein gp120
-
HLA-D Antigens
-
Peptide Fragments
-
Recombinant Proteins