Profound alteration in an alpha beta T-cell antigen receptor repertoire due to polymorphism in the first complementarity-determining region of the beta chain.
Profound alteration in an alpha beta T-cell antigen receptor repertoire due to polymorphism in the first complementarity-determining region of the beta chain.
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由于 β 链第一个互补决定区的多态性，αβ T 细胞抗原受体库发生了深刻的改变。
DOI：
10.1073/pnas.88.22.10267
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发表时间：
1991
影响因子：
11.1
通讯作者：
Matis,LA
中科院分区：
文献类型：
--
作者：
Gahm,SJ;Fowlkes,BJ;Jameson,SC;Gascoigne,NR;Cotterman,MM;Kanagawa,O;Schwartz,RH;Matis,LA
在维持免疫球蛋白重链和轻链可变（V）区的框架结构中至关重要的氨基酸残基在α β T细胞抗原受体（TCR α β）的V α和V β蛋白中是高度保守的。因此，已经提出TCR α β具有与免疫球蛋白Fab片段相似的构象，并且与三个免疫球蛋白互补决定区（CDR 1、2和3）同源的TCR区域结合肽抗原-主要组织相容性复合物（MHC）分子配体。某些小鼠品系的V β 3蛋白的预测CDR 1中的单个氨基酸取代显著改变了抗原特异性MHC限制性免疫应答中TCR α β的使用，但没有消除V β 3对超抗原次要淋巴细胞刺激位点（Mls）c和葡萄球菌肠毒素A（SEA）的特异性。结果证实了V β CDR 1在抗原-MHC分子识别中的重要性，支持TCR α β的Fab样结构模型，并提供了进一步的证据，即常规抗原-MHC识别和超抗原识别是由TCR β链的不同区域介导的。他们还表明，等位基因多态性可能是TCR库多样性的重要来源。
Amino acid residues that are critical in maintaining the framework structure of immunoglobulin heavy- and light-chain variable (V) regions are strongly conserved in the V alpha and V beta proteins of the alpha beta T-cell antigen receptor (TCR alpha beta). Consequently, it has been proposed that TCR alpha beta has a conformation similar to that of an immunoglobulin Fab fragment and that the regions of the TCR homologous to the three immunoglobulin complementarity-determining regions (CDRs 1, 2, and 3) bind to the peptide antigen-major histocompatibility complex (MHC) molecule ligand. A single amino acid substitution in the predicted CDR1 of the V beta 3 protein of certain mouse strains dramatically altered TCR alpha beta usage in an antigen-specific MHC-restricted immune response but did not abrogate V beta 3 specificity for the superantigens minor lymphocyte stimulatory locus (Mls)c and staphylococcal enterotoxin A (SEA). The results confirm the importance of the V beta CDR1 in antigen-MHC molecule recognition, supporting the Fab-like structural model of TCR alpha beta, and provide further evidence that conventional antigen-MHC recognition and superantigen recognition are mediated by distinct regions of the TCR beta chain. They also suggest that allelic polymorphism may be a significant source of diversity in the TCR repertoire.