SOLUTION STRUCTURE OF HUMAN CTLA-4 AND DELINEATION OF A CD80 CD86 BINDING-SITE CONSERVED IN CD28/

Authors
METZLER WJ BAJORATH J FENDERSON W SHAW SY CONSTANTINE KL NAEMURA J LEYTZE G PEACH RJ LAVOIE TB MUELLER L LINSLEY PS
Citation
Wj. Metzler et al., SOLUTION STRUCTURE OF HUMAN CTLA-4 AND DELINEATION OF A CD80 CD86 BINDING-SITE CONSERVED IN CD28/, Nature structural biology, 4(7), 1997, pp. 527-531
Citations number
27
Categorie Soggetti
Biology,"Cell Biology
Journal title
Nature structural biology → ACNP
ISSN journal
10728368
Volume
4
Issue
7
Year of publication
1997
Pages
527 - 531
Database
ISI
SICI code
1072-8368(1997)4:7<527:SSOHCA>2.0.ZU;2-N
Abstract
The structure of human CTLA-4 reveals that residues Met 99, Tyr 100 an d 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, significantl y reduces binding to CD80 and/or CD86, implicating this patch as a lig and binding site.