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Crystal structure of a gamma delta t cell receptor ligand t22: A truncated mhc-like fold

Academic Article
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Overview

authors

  • Wingren, C.
  • Crowley, M. P.
  • Degano, M.
  • Chien, Y. H.
  • Wilson, Ian

publication date

  • January 2000

journal

  • Science  Journal

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.

subject areas

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

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.287.5451.310

PubMed ID

  • 10634787
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Additional Document Info

start page

  • 310

end page

  • 314

volume

  • 287

issue

  • 5451

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