Abstract
Murine T10 and T22 are highly related nonclassical major histocompatibility complex (MHC) class Ib proteins that bind to certain gammadelta 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 gammadelta 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 gammadelta and alphabeta TCRs interact differently with their respective MHC ligands.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alleles
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Amino Acid Substitution
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Animals
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Binding Sites
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Crystallography, X-Ray
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Glycosylation
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Histocompatibility Antigens Class I / chemistry*
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Hydrogen Bonding
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Ligands
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Mice
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Models, Molecular
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Point Mutation
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Protein Conformation
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Protein Folding
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / immunology
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Proteins / metabolism
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Receptors, Antigen, T-Cell, gamma-delta / immunology
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Receptors, Antigen, T-Cell, gamma-delta / metabolism*
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Surface Properties
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beta 2-Microglobulin / chemistry
Substances
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Histocompatibility Antigens Class I
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Ligands
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Proteins
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Receptors, Antigen, T-Cell, gamma-delta
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beta 2-Microglobulin
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T22 antigen