MUTATIONAL ANALYSIS OF THE INTERACTION BETWEEN CD4 AND CLASS-II MHC - CLASS-II ANTIGENS CONTACT CD4 ON A SURFACE OPPOSITE THE GP120-BINDING SITE
MUTATIONAL ANALYSIS OF THE INTERACTION BETWEEN CD4 AND CLASS-II MHC - CLASS-II ANTIGENS CONTACT CD4 ON A SURFACE OPPOSITE THE GP120-BINDING SITE
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DOI：
10.1016/0092-8674(91)90447-7
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发表时间：
1991-09-06
期刊：
影响因子：
64.5
通讯作者：
SEKALY, RP
中科院分区：
文献类型：
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作者：
FLEURY, S;LAMARRE, D;SEKALY, RP
使用功能和粘附试验，我们已经研究了30人CD 4突变体的能力，与II类主要组织相容性复合体（MHC）分子，也与人类免疫缺陷病毒的gp 120相互作用。突变体覆盖了CD 4的四个结构域（D1-D4），并包括几个单位点取代。在CD 4晶体结构的背景下，结果分析表明，影响与II类MHC分子相互作用的突变位于CD 4结构域1和2的三个暴露环上。特别涉及的残基19、89和165在CD 4分子的一面上彼此分开9埃、24埃和24埃。此外，II类结合位点不包括CD 4分子的残基43至49，即已知参与gp 120结合的相对面上的区域。
Using functional and adhesion assays, we have studied the ability of 30 human CD4 mutants to interact with class II major histocompatibility complex (MHC) molecules and also with gp120 from human immunodeficiency virus. The mutants cover the four domains (D1-D4) of CD4 and include several single-site substitutions. Analysis of the results, in the context of the CD4 crystal structure, shows that mutations that affect the interaction with class II MHC molecules are located on three exposed loops from CD4 domains 1 and 2. The specifically implicated residues, 19, 89, and 165, are separated from one another by 9 angstrom, 24 angstrom, and 24 angstrom on one face of the CD4 molecule. Moreover, the class II binding site does not include residues 43 to 49 of the CD4 molecule, a region on an opposite face known to be involved in the binding of gp120.