人CD4的HIV结合重组片段的晶体结构
Crystal structure of an HIV-binding recombinant fragment of human CD4.
作者信息
Ryu S E, Kwong P D, Truneh A, Porter T G, Arthos J, Rosenberg M, Dai X P, Xuong N H, Axel R, Sweet R W
机构信息
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
出版信息
Nature. 1990 Nov 29;348(6300):419-26. doi: 10.1038/348419a0.
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.
摘要
T细胞表面的CD4糖蛋白有助于免疫反应，并且是HIV感染的受体。以2.3埃分辨率测定的CD4可溶性片段的结构表明，该分子有两个紧密相连的免疫球蛋白样结构域。通过对突变体和抗体结合的分析表明，与HIV识别相关的残基是结构域D1的显著特征。结构域D2的特点是其β链拓扑结构不同于抗体结构域，且存在一个片内二硫键。
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