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Crystal Structure of a γδ T Cell Receptor Ligand T22: A Truncated MHC-Like Fold

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Science  14 Jan 2000:
Vol. 287, Issue 5451, pp. 310-314
DOI: 10.1126/science.287.5451.310

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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 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 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.

  • * Present address: Department of Immunotechnology, Lund University, Post Office Box 7031, SE-22007 Lund, Sweden.

  • Present address: Structural Biology Laboratory, Sincrotrone Trieste in Area Science Park, S.S. 14 Km 163.5, 34012 Basovizza (TS), Italy.

  • § To whom correspondence should be addressed. E-mail: wilson{at}scripps.edu

  • Present address: Howard Hughes Medical Institute, Duke Medical Center, Durham, NC 27706, USA.

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