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

Nature volume 348, pages 419–426 (1990)Cite this article

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 Å 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 Dl. Domain D2 is distinguished by a variation on the β-strand topologies of antibody domains and by an intra-sheet disulphide bridge.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York, 10032, USA

    Seong-Eon Ryu, Peter D. Kwong, Richard Axel & Wayne A. Hendrickson

  2. Howard Hughes Medical Institute, Columbia University, New York, New York, 10032, USA

    Richard Axel & Wayne A. Hendrickson

  3. SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania, 19406, USA

    Alemseged Truneh, Terence G. Porter, James Arthos, Martin Rosenberg & Raymond W. Sweet

  4. Departments of Physics, Chemistry and Biology, University of California at San Diego, La Jolla, California, 90293, USA

    Xiaoping Dai & Nguyen-huu Xuong

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  1. Seong-Eon Ryu
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Ryu, SE., Kwong, P., Truneh, A. et al. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature 348, 419–426 (1990). https://doi.org/10.1038/348419a0

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