Structural highlights
Function
Q31615_MOUSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold.,Wingren C, Crowley MP, Degano M, Chien Y, Wilson IA Science. 2000 Jan 14;287(5451):310-4. PMID:10634787[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wingren C, Crowley MP, Degano M, Chien Y, Wilson IA. Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold. Science. 2000 Jan 14;287(5451):310-4. PMID:10634787