Nature. 1990 Nov 29;348(6300):419-26.

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

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

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

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.

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Immunology. One hand clapping. [Nature. 1990]
Immunology. One hand clapping.Travers P. Nature. 1990 Nov 29; 348(6300):393-4.

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Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. [Nature. 1990]
Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains.
Wang JH, Yan YW, Garrett TP, Liu JH, Rodgers DW, Garlick RL, Tarr GE, Husain Y, Reinherz EL, Harrison SC. Nature. 1990 Nov 29; 348(6300):411-8.
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Crystal structure of an HIV-binding recombinant fragment of human CD4.
Crystal structure of an HIV-binding recombinant fragment of human CD4.
Nature. 1990 Nov 29 ;348(6300):419-26.

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