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• W2023403245 endingPage "1230" @default.
• W2023403245 startingPage "1223" @default.
• W2023403245 abstract "Recent studies have shown that many nonclassical major histocompatibility complex (MHC) (class 1b) 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 beta2-microglobulin (beta2m) 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 gammadelta T cell clone, G8. Circular dichroism analysis indicates that T10/beta2m 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." @default.
• W2023403245 created "2016-06-24" @default.
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• W2023403245 date "1997-04-07" @default.
• W2023403245 modified "2023-09-23" @default.
• W2023403245 title "The Recognition of the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule, T10, by the γδ T Cell, G8" @default.
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• W2023403245 doi "https://doi.org/10.1084/jem.185.7.1223" @default.
• W2023403245 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2196254" @default.
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