Crystal structure of an HIV-binding recombinant fragment of human CD4.
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.
Ryu
S E
SE
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Kwong
P D
PD
Truneh
A
A
Porter
T G
TG
Arthos
J
J
Rosenberg
M
M
Dai
X P
XP
Xuong
N H
NH
Axel
R
R
Sweet
R W
RW
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D005075:Biological Evolution; D015704:CD4 Antigens / Q000648:ultrastructure*; D003196:Computer Graphics; D003461:Crystallography; D004252:DNA Mutational Analysis; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D006681:HLA-D Antigens / Q000378:metabolism; D008561:Membrane Fusion; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010446:Peptide Fragments; D011487:Protein Conformation; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D000911:Antibodies, Monoclonal; D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D006681:HLA-D Antigens; D010446:Peptide Fragments; D011994:Recombinant Proteins