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

Autor:	Keith L. Constantine, Luciano Mueller, Peter S. Linsley, Robert J. Peach, Jürgen Bajorath, Thomas B. Lavoie, William Fenderson, Gina Leytze, William J. Metzler, Shyh Yu Shaw, Naemura Joseph R
Rok vydání:	1997
Předmět:	Models Molecular Immunoconjugates Magnetic Resonance Spectroscopy Stereochemistry Protein Conformation Molecular Sequence Data chemical and pharmacologic phenomena Biology Sulfides Biochemistry Conserved sequence Abatacept Protein structure CD28 Antigens Structural Biology Antigens CD Genetics Animals Humans CTLA-4 Antigen Amino Acid Sequence Binding site Peptide sequence Conserved Sequence CD86 chemistry.chemical_classification Binding Sites Membrane Glycoproteins Sequence Homology Amino Acid CD28 hemic and immune systems Antigens Differentiation Amino acid Solutions chemistry B7-1 Antigen B7-2 Antigen Dimerization CD80
Zdroj:	Nature structural biology. 4(7)
ISSN:	1072-8368
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::133e3496fe730a479ed75768daded08b https://pubmed.ncbi.nlm.nih.gov/9228944 Zobrazit plný text záznamu Full text from SpringerLink