人CTLA-4的溶液结构以及CD28中保守的CD80/CD86结合位点的描绘。
Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28.
作者信息
Metzler W J, Bajorath J, Fenderson W, Shaw S Y, Constantine K L, Naemura J, Leytze G, Peach R J, Lavoie T B, Mueller L, Linsley P S
出版信息
Nat Struct Biol. 1997 Jul;4(7):527-31. doi: 10.1038/nsb0797-527.
PMID:9228944
Abstract
The structure of human CTLA-4 reveals that residues Met 99, Tyr 100 and Tyr 104 of the M99YPPPY104 motif are adjacent to a patch of charged surface residues on the A'GFCC' face of the protein. Mutation of these residues, which are conserved in the CTLA-4/CD28 family, significantly reduces binding to CD80 and/or CD86, implicating this patch as a ligand binding site.
摘要
人类CTLA-4的结构显示，M99YPPPY104基序中的甲硫氨酸99、酪氨酸100和酪氨酸104残基毗邻该蛋白A'GFCC'面上的一片带电荷的表面残基。这些在CTLA-4/CD28家族中保守的残基发生突变，会显著降低与CD80和/或CD86的结合，表明这片区域是一个配体结合位点。
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