Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28

被引：119

作者：

Metzler, WJ

Bajorath, J

Fenderson, W

Shaw, SY

Constantine, KL

Naemura, J

Leytze, G

Peach, RJ

Lavoie, TB

Mueller, L

Linsley, PS

机构：

[1] BRISTOL MYERS SQUIBB PHARMACEUT RES INST,DEPT PEPTIDE & PROT RES,PRINCETON,NJ 08543

[2] BRISTOL MYERS SQUIBB PHARMACEUT RES INST,DEPT INFLAMMAT,SEATTLE,WA 98121

[3] BRISTOL MYERS SQUIBB PHARMACEUT RES INST,DEPT IMMUNOMODULAT,SEATTLE,WA 98121

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 07期

关键词：

D O I：

10.1038/nsb0797-527

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：527 / 531

页数：5

共 27 条

[1] MEASUREMENT OF LONG-RANGE C-13-C-13 J COUPLINGS IN A 20-KDA PROTEIN-PEPTIDE COMPLEX [J].