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Science 14 January 2000:
Vol. 287. no. 5451, pp. 310 - 314
DOI: 10.1126/science.287.5451.310

Reports

Crystal Structure of a gamma &dgr; T Cell Receptor Ligand T22: A Truncated MHC-Like Fold

Christer Wingren, 1* Michael P. Crowley, 2 † Massimo Degano, 1ddagger Yueh-hsiu Chien, 2 Ian A. Wilson 1§

Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gamma delta 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 gamma delta 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 gamma delta and alpha beta TCRs interact differently with their respective MHC ligands.

1 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.
2 Program of Immunology and the Department of Microbiology and Immunology, Stanford University, School of Medicine, Stanford, CA 94305, USA.
*   Present address: Department of Immunotechnology, Lund University, Post Office Box 7031, SE-22007 Lund, Sweden.

ddagger    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


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