Ghosh P, Amaya M, Mellins E, Wiley D C
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Nature. 1995 Nov 30;378(6556):457-62. doi: 10.1038/378457a0.
A complex between HLA-DR3 and a fragment of invariant chain called CLIP was isolated from a human cell line defective in antigen presentation and its X-ray crystal structure determined. Previous data indicate that this complex is an intermediate in class II histocompatibility maturation, occurring between invariant chain-DR3 and antigenic peptide-DR3 complexes. The structure shows that the CLIP fragment binds to DR3 in a way almost identical to that in which antigenic peptides bind class II histocompatibility glycoproteins. The structure is the substrate for the loading of antigenic peptides by an exchange process catalysed by DM.
从一个抗原呈递缺陷的人类细胞系中分离出了一种HLA - DR3与一种名为CLIP的恒定链片段的复合物，并确定了其X射线晶体结构。先前的数据表明，这种复合物是II类组织相容性成熟过程中的一个中间体，出现在恒定链 - DR3复合物和抗原肽 - DR3复合物之间。该结构显示，CLIP片段与DR3的结合方式几乎与抗原肽与II类组织相容性糖蛋白的结合方式相同。该结构是由DM催化的交换过程中抗原肽加载的底物。
