Bentley G A, Boulot G, Karjalainen K, Mariuzza R A
Unite d'Immunologie Structurale (CNRS URA 359), Institut Pasteur, Paris, France.
Science. 1995 Mar 31;267(5206):1984-7. doi: 10.1126/science.7701320.
The crystal structure of the extracellular portion of the beta chain of a murine T cell antigen receptor (TCR), determined at a resolution of 1.7 angstroms, shows structural homology to immunoglobulins. The structure of the first and second hypervariable loops suggested that, in general, they adopt more restricted sets of conformations in TCR beta chains than those found in immunoglobulins; the third hypervariable loop had certain structural characteristics in common with those of immunoglobulin heavy chain variable domains. The variable and constant domains were in close contact, presumably restricting the flexibility of the beta chain. This may facilitate signal transduction from the TCR to the associated CD3 molecules in the TCR-CD3 complex.
以1.7埃的分辨率测定的小鼠T细胞抗原受体(TCR)β链胞外部分的晶体结构显示出与免疫球蛋白的结构同源性。第一和第二高变环的结构表明,总体而言,它们在TCRβ链中采用的构象集比在免疫球蛋白中发现的构象集更受限;第三高变环具有与免疫球蛋白重链可变结构域的某些结构特征相同之处。可变结构域和恒定结构域紧密接触,推测这限制了β链的灵活性。这可能有助于从TCR向TCR-CD3复合物中的相关CD3分子进行信号转导。