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PMID: 2247146 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Crystal structure of an HIV-binding recombinant fragment of human CD4.

Nature ·Vol. 348 ·No. 6300 ·1990-11-29 ·Pages 419-26

Ryu SE, Kwong PD, Truneh A, Porter TG, Arthos J, Rosenberg M, Dai XP, Xuong NH, Axel R, Sweet RW

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.

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
Chemicals
Antibodies, Monoclonal CD4 Antigens HIV Envelope Protein gp120 HLA-D Antigens Peptide Fragments Recombinant Proteins
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Ryu S E
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Kwong P D
Truneh A
Porter T G
Arthos J
Rosenberg M
Dai X P
Xuong N H
Axel R
Sweet R W
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Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1990-11-29
Pages
419-26
Language
English
Region
England
NLM ID
0410462
PMCID
PMC5638305
Subset
IM
Grants
NIGMS NIH HHS · R01 GM034102 · United States
Corrections
CommentIn
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