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首页> 外文期刊>Journal of Molecular Biology >DUAL CONFORMATIONS OF A T CELL RECEPTOR V-ALPHA HOMODIMER - IMPLICATIONS FOR VARIABILITY IN V-ALPHA-V-BETA DOMAIN ASSOCIATION
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DUAL CONFORMATIONS OF A T CELL RECEPTOR V-ALPHA HOMODIMER - IMPLICATIONS FOR VARIABILITY IN V-ALPHA-V-BETA DOMAIN ASSOCIATION

机译：T细胞受体V-α均聚物的双重构象-V-Alpha-V-BETA域关联的变异性

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摘要

The crystal structure of a mutant T cell receptor (TCR) V alpha domain containing a grafted third complementarity-determining region (CDR3) from a different V alpha was determined at 2.3 Angstrom resolution by molecular replacement using the wild-type V alpha structure as a search model. Like the wild-type V alpha domain, the mutant crystallized as a homodimer very similar to TCR V alpha V beta and antibody VLVH heterodimers, with the CDR loops disposed to form part of the antigen-binding site. However, the relative orientation of the two chains in the mutant V alpha homodimer differs from that in the wild-type by a rotation of 14 degrees such that the buried surface area in the dimer interface of the mutant is 140 Angstrom(2) less than in the wildtype. While the residues forming the interface are essentially the same in the two structures, there are only four pairs of interface hydrogen bonds in the case of the mutant compared with eight for the wild-type. These results suggest that multiple relative orientations of the V alpha and V beta domains of TCRs may be possible, providing a significant contribution to TCR combining site diversity. (C) 1997 Academic Press Limited. [References: 37]
机译：使用野生型Vα结构作为分子置换，以2.3埃的分辨率确定了包含来自不同Vα的嫁接的第三互补决定区（CDR3）的突变T细胞受体（TCR）Vα结构域的晶体结构。搜索模型。像野生型Vα域一样，该突变体结晶为同二聚体，与TCR VαVβ和抗体VLVH异二聚体非常相似，而CDR环则形成了抗原结合位点的一部分。但是，突变体V alpha同型二聚体中两条链的相对取向与野生型中的两条链的相对取向相差14度，使得突变体的二聚体界面中的埋入表面积小于140埃（2）。在野生型中。尽管形成界面的残基在两个结构中基本相同，但在突变体的情况下只有四对界面氢键，而野生型则为八对。这些结果表明，TCR的V alpha和V beta域的多个相对方向是可能的，这为结合位点多样性的TCR提供了重要的贡献。 （C）1997 Academic Press Limited。 [参考：37]

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