| Literature DB >> 9228944 |
W J Metzler, J Bajorath, W Fenderson, S Y Shaw, K L Constantine, J Naemura, G Leytze, R J Peach, T B Lavoie, L Mueller, P S Linsley.
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.Entities:
Mesh：
Substances：
Year: 1997 PMID： 9228944 DOI： 10.1038/nsb0797-527
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368