J. Exp. Med.
© The Rockefeller University Press
0022-1007/97/04/1223/08 $2.00
Volume 185, Number 7, April 7, 1997 1223-1230

The Recognition of the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule, T10, by the T Cell, G8

By Michael P. Crowley,^* Ziv Reich, Nasim Mavaddat,^§ John D. Altman,^§ and Yueh-hsiu Chien^*§

From the ^* Program in Immunology;  The Howard Hughes Medical Institute; and the ^§ Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305

Recent studies have shown that many nonclassical major histocompatibility complex (MHC) (class Ib) molecules have distinct antigen-binding capabilities, including the binding of nonpeptide moieties and the binding of peptides that are different from those bound to classical MHC molecules. Here, we show that one of the H-2T region-encoded molecules, T10, when produced in Escherichia coli, can be folded in vitro with ₂-microglobulin (₂m) to form a stable heterodimer in the absence of peptide or nonpeptide moieties. This heterodimer can be recognized by specific antibodies and is stimulatory to the T cell clone, G8. Circular dichroism analysis indicates that T10/₂m has structural features distinct from those of classical MHC class I molecules. These results suggest a new way for MHC-like molecules to adopt a peptide-free structure and to function in the immune system.

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