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 rec...

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Bibliographic Details
Published in:Nature (London) 1990-11, Vol.348 (6300), p.419-426
Main Authors: Ryu, Seong-Eon, Kwong, Peter D, Truneh, Alemseged, Porter, Terence G, Arthos, James, Rosenberg, Martin, Dai, Xiaoping, Xuong, Nguyen-huu, Axel, Richard, Sweet, Raymond W, Hendrickson, Wayne A
Format: Article
Language:English
Subjects:
Acquired immune deficiency syndrome
AIDS
Amino Acid Sequence
Antibodies
Antibodies, Monoclonal - immunology
Antigenic determinants, haptens, artificial antigens
Antigens
Binding
Binding Sites
Biochemistry
Biological and medical sciences
Biological Evolution
CD4 antigen
CD4 Antigens - ultrastructure
Cellular biology
Computer Graphics
Crystal structure
Crystallography
DNA Mutational Analysis
Domains
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Glycoproteins
HIV
HIV Envelope Protein gp120 - metabolism
HLA-D Antigens - metabolism
Human immunodeficiency virus
Immune response
Immune system
Immunity (Disease)
Immunoglobulins
Infections
Lymphocytes
Lymphocytes T
Medical research
Membrane Fusion
Models, Molecular
Molecular immunology
Molecular Sequence Data
Molecular Structure
Mutants
Peptide Fragments
Polyethylene glycol
Protein Conformation
Proteins
Recombinant Proteins
Solvents
Structure-Activity Relationship
Topology
Viral infections
X-ray crystallography
X-Ray Diffraction
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/348419a0