Crystal Structure of a γδ T Cell Receptor Ligand T22: A Truncated MHC-Like Fold
Authors:
- 14 January 2000
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 287 (5451) , 310-314
Abstract
Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain γδ T cell receptors (TCRs) in the absence of other components. The crystal structure of T22 b 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 β-sheet floor. Potential γδ 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 γδ and αβ TCRs interact differently with their respective MHC ligands.Keywords
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