Crystal structure of an HIV-binding recombinant fragment of human CD4
1990; Nature Portfolio; Volume: 348; Issue: 6300 Linguagem: Inglês
10.1038/348419a0
ISSN1476-4687
AutoresSeong-Eon Ryu, Peter D. Kwong, Alemseged Truneh, Terence G. Porter, James Arthos, Martin Rosenberg, Xiaoping Dai, Nguyen-huu Xuong, Richard Axel, Raymond W. Sweet, Wayne A. Hendrickson,
Tópico(s)Immune Cell Function and Interaction
ResumoCD4 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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