Structural characterization of the TCR complex by electron microscopy

Ignacio Arechaga, Mahima Swamy, David Abia, Wolfgang A. Schamel (Lead / Corresponding author), Balbino Alarcón, José María Valpuesta

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Structural information on how the TCR transmits signals upon binding of its antigen peptide MHC molecule ligand is still lacking. The ectodomains of the TCRα/β, CD3∈γ and CD3∈δ dimers, as well as the transmembrane domain of CD3ζ, have been characterized by X-ray crystallography and nuclear magnetic resonance (NMR). However, no structural data have been obtained for the entire TCR complex. In this study, we have purified the TCR from T cells under native conditions and used electron microscopy to derive a three-dimensional structure. The TCR complex appears as a pear-shaped structure of 180 × 120 × 65 Å Furthermore, the use of mAbs has allowed to determine the orientation of the TCRα/β and CD3 subunits and to suggest a model of interactions. Interestingly, the reconstructed TCR is larger than expected for a complex with a αβγ∈δ∈ζζ stoichiometry. The accommodation of a second TCRαβ to fill in the extra volume is discussed.

Original languageEnglish
Pages (from-to)897-903
Number of pages7
JournalInternational Immunology
Volume22
Issue number11
DOIs
Publication statusPublished - 1 Nov 2010

Keywords

  • CD3
  • Purification
  • Structure
  • TCR

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