Summary
PDB 1AH1 deposited: 1997-04-11 modified: 2011-07-13
Title CTLA-4, NMR, 20 STRUCTURES
Authors Bajorath, J., Constantine, K.L., Fenderson, W., Lavoie, T.B., Leytze, G., Linsley, P.S., Metzler, W.J., Mueller, L., Naemura, J., Peach, R.J., Shaw, S.Y.
Method SOLUTION NMR
Structure factors resolution None rfactor None rfree None
DPI
Citations

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.

Nat.Struct.Biol. 1997 Jul; 4(7):527-531 doi:10.1038/nsb0797-527

Cross References
Database source Identifier Description
PubMed 9228944 NSBIEW
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1AH1/0 1AH1 0 monomer 0 1 8 1006