Jardetzky T S, Brown J H, Gorga J C, Stern L J, Urban R G, Chi Y I, Stauffacher C, Strominger J L, Wiley D C
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Nature. 1994 Apr 21;368(6473):711-8. doi: 10.1038/368711a0.
The structure of a bacterial superantigen, Staphylococcus aureus enterotoxin B, bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography. The superantigen binds as an intact protein outside the conventional peptide antigen-binding site of the class II major histocompatibility complex (MHC) molecule. No large conformational changes occur upon complex formation in either the DR1 or the enterotoxin B molecules. The structure of the complex helps explain how different class II molecules and superantigens associate and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.
通过X射线晶体学已确定了与人类II类组织相容性复合体分子（HLA - DR1）结合的细菌超抗原——金黄色葡萄球菌肠毒素B的结构。该超抗原作为完整蛋白质结合在II类主要组织相容性复合体（MHC）分子的传统肽抗原结合位点之外。在形成复合物时，DR1分子或肠毒素B分子均未发生大的构象变化。该复合物的结构有助于解释不同的II类分子与超抗原如何结合，并提出了与T细胞抗原受体（TCR）形成三元复合物的模型，其中TCR与MHC的非常规接触是可能的。
