MOUSE T CELL RECEPTORS SPECIFIC FOR VESICULAR STOMATITIS VIRUS & HIV CD4 STRUCT

多个小鼠T细胞的三维结构解析 与K蛋白结合的病毒八肽(VSV8)的细胞受体 B MHC I类分子 T细胞识别病毒、细菌的细胞相关病原体[或 真菌起源和肿瘤抗原通过一种独特的分子 被称为T细胞受体(TCR)。TCR综合体包括 T淋巴细胞表面的多个跨膜链。 二硫键连接的α-P杂二聚体是一种克隆性独特的成分，它 在重大疾病的背景下拥有抗原的识别位置 组织相容性复合体(MHC)，而不变的CD3成分 (y、6、e和q参与信号转导。因为 这种复合体的紧密膜缔合，分子的研究 TCR识别的特征必然是间接的。 最近为了解这一承认过程的性质所作的努力 都把重点放在了系统的结构研究上。众所周知， 几年来，I类和11类MHC分子，尽管 这两个亚基的化学成分非常不同， 相同的拓扑结构“-S，尤其是MHC分子 目前的抗原肽是相似的。一种短的抗原肽 (第I类为8-10个残基，第11类为12个残基)位于 MHC分子顶部的大凹槽。这条沟槽是由 八股反平行P片作为地板，两股 反平行的a型螺旋作为侧壁。在I类MHC分子中， 整个凹槽由来自相同a链的区域a1和a2形成； 11类MHC分子，凹槽由结构域al和01形成 两个不同的链(a和0)。多肽的结构细节 与这些MHC分子具有高亲和力的结合一直很好 特色化的。

To solve the three dimensional structures of multiple murine T cell receptors specific for a viral octapeptide (VSV8) bound to the K b MHC class I molecule T cells recognize cell-associated pathogens of viral, bacteria[ or fungal origin as well as tumor antigens through a unique molecule termed the T cell receptor (TCR). The TCR complex consists of multiple transmembrane chains on the surface of T lymphocytes',". The disulfide-linked a-P heterodimer is a clonally unique component that possesses a recognition site for antigen in the context of the major histocompatibility complex (MHC), while the invariant CD3 components (y, 6, e, and Q are involved in signal transduction. Because of the intimate membrane association of this complex, study of the molecular features of TCR recognition necessarily have been indirect. Recent efforts to understand the nature of this recognition process have focused on structural studies of the system. It has been known for a few years that both class I and class 11 MHC molecules, despite the very different chemical compositions of the two subunits, have the same topologic structure"-s. in particular, the way MHC molecules present the antigenic peptide is similar. A short antigenic peptide (8-10 residues for class I and >1 2 residues for class 11) lies in a large groove at the top of the MHC molecule. This groove is composed of eight strands of anti-parallel P-sheet as a floor, and two anti-parallel a-helices as side walls. In class I MHC molecules, the whole groove is formed by domain al and a2 from the same a chain; in class 11 MHC molecules, the groove is formed by domain al, and 01 from two different chains (a and 0). Structural details of how peptides bind with high affinity to these MHC molecules have been well characterized.