CD8与主要组织相容性复合体（MHC）I类分子之间的相互作用由多个接触表面介导，这些接触表面包括MHC I类分子的α2和α3结构域。
Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I.
作者信息
Sun J, Leahy D J, Kavathas P B
机构信息
Department of Laboratory Medicine, Yale University School of Medicine, New Haven, Connecticut 06520-8035, USA.
出版信息
J Exp Med. 1995 Nov 1;182(5):1275-80. doi: 10.1084/jem.182.5.1275.
Abstract
The cell surface glycoprotein CD8 functions as a coreceptor with the TCR on cytotoxic T lymphocytes. Mutational analysis of the binding site of CD8 for MHC class I predicted that distinct surfaces of CD8 would interact with both the alpha 2 and alpha 3 domains of class I. Using a cell-cell adhesion assay, we identified three residues Q115, D122, and E128 in the alpha 2 domain of class I critical for interaction with CD8. The side chains of these residues point towards a cavity formed by the alpha 1/alpha 2 platform, the alpha 3 domain and beta 2-microglobulin (beta 2m) of class I. These residues were predicted to contact CD8 based on a bivalent model of interaction between one CD8 alpha/alpha homodimer and two MHC class I molecules. These results therefore provide support for the model.
摘要
细胞表面糖蛋白CD8作为细胞毒性T淋巴细胞上与TCR共同起作用的受体。对CD8与I类主要组织相容性复合体（MHC）结合位点的突变分析预测，CD8的不同表面会与I类的α2和α3结构域相互作用。利用细胞-细胞黏附试验，我们在I类的α2结构域中鉴定出三个对与CD8相互作用至关重要的残基Q115、D122和E128。这些残基的侧链指向由I类的α1/α2平台、α3结构域和β2微球蛋白（β2m）形成的一个腔。基于一个CD8α/α同二聚体与两个I类MHC分子之间相互作用的二价模型，预测这些残基会与CD8接触。因此，这些结果为该模型提供了支持。
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