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Science 14 January 2000: Vol. 287. no. 5451, pp. 310 - 314 DOI: 10.1126/science.287.5451.310
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Reports
Crystal Structure of a  T Cell Receptor Ligand T22: A Truncated MHC-Like Fold
Christer Wingren,
1*
Michael P. Crowley,
2
Massimo Degano,
1
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  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 -sheet floor. Potential  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  and  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.
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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