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Crystal structure of an HIV-binding recombinant fragment of human CD4.
- Source :
-
Nature [Nature] 1990 Nov 29; Vol. 348 (6300), pp. 419-26. - Publication Year :
- 1990
-
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.
- Subjects :
- Amino Acid Sequence
Antibodies, Monoclonal immunology
Binding Sites
Biological Evolution
Computer Graphics
Crystallography
DNA Mutational Analysis
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
CD4 Antigens ultrastructure
HIV Envelope Protein gp120 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 348
- Issue :
- 6300
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 2247146
- Full Text :
- https://doi.org/10.1038/348419a0