Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold.
Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta T cell receptors (TCRs) in the absence of other components. The crystal structure of T22b at 3.1 angstroms reveals similarities to MHC class I molecules, but one side of the normal peptide-binding groove is severely truncated, which allows direct access to the beta-sheet floor. Potential gammadelta TCR-binding sites can be inferred from functional mapping of T10 and T22 point mutants and allelic variants. Thus, T22 represents an unusual variant of the MHC-like fold and indicates that gammadelta and alphabeta TCRs interact differently with their respective MHC ligands.
Wingren
C
C
Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Crowley
M P
MP
Degano
M
M
Chien
Y
Y
Wilson
I A
IA
D000483:Alleles; D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006031:Glycosylation; D015395:Histocompatibility Antigens Class I / Q000737:chemistry*; D006860:Hydrogen Bonding; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D017354:Point Mutation; D011487:Protein Conformation; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D016692:Receptors, Antigen, T-Cell, gamma-delta / Q000276:immunology / Q000378:metabolism*; D013499:Surface Properties; D001613:beta 2-Microglobulin / Q000737:chemistry
D015395:Histocompatibility Antigens Class I; D008024:Ligands; D011506:Proteins; D016692:Receptors, Antigen, T-Cell, gamma-delta; D001613:beta 2-Microglobulin; C089395:T22 antigen