Crystal structure of a gammadelta T cell receptor ligand T22: a truncated MHC-like fold

Science. 2000 Jan 14;287(5451):310-4. doi: 10.1126/science.287.5451.310.


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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alleles
  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • Crystallography, X-Ray
  • Glycosylation
  • Histocompatibility Antigens Class I / chemistry*
  • Hydrogen Bonding
  • Ligands
  • Mice
  • Models, Molecular
  • Point Mutation
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / immunology
  • Proteins / metabolism
  • Receptors, Antigen, T-Cell, gamma-delta / immunology
  • Receptors, Antigen, T-Cell, gamma-delta / metabolism*
  • Surface Properties
  • beta 2-Microglobulin / chemistry


  • Histocompatibility Antigens Class I
  • Ligands
  • Proteins
  • Receptors, Antigen, T-Cell, gamma-delta
  • beta 2-Microglobulin
  • T22 antigen

Associated data

  • PDB/1C16