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An alternative conformation of the T-cell receptor alpha constant region.

机译:T细胞受体α恒定区的另一种构象。

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Alphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, which recognizes the autoantigen myelin basic protein. The 2.0-A-resolution structure reveals canonical main-chain conformations for the V(alpha), V(beta), and C(beta) domains, but the C(alpha) domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE beta-turns results in beta-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of "metamorphic proteins."
机译:字母T细胞受体(TcRs)在细胞免疫反应中起着核心作用。它们是Ig超家族的成员,α和β链的胞外区域各包含一个V型结构域和一个C型结构域。我们已经确定了字母TcR的胞外域结构,该结构识别自身抗原髓鞘碱性蛋白。 2.0-A分辨率结构揭示了Vα,Vβ和Cβ域的规范主链构象,但Cα域显示的主链构象与以前的显着不同报道了TcR晶体结构。保持了整体的IgC样折叠,但BC和DE的β形转弯之间的活塞式重排导致β链滑动。这种基本的构象变化可以代表信号中间体。我们的结构是人们日益认可的“变形蛋白”概念的Ig折叠的第一个例子。

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