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Int Immunol. 2010 Nov;22(11):897-903. doi: 10.1093/intimm/dxq443. Epub 2010 Nov 8.

Structural characterization of the TCR complex by electron microscopy.

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Departamento de Biología Molecular, Universidad de Cantabria (UC) and Instituto de Biomedicina y Biotecnología de Cantabria, IBBTEC (CSIC-UC-IDICAN), c/Herrera Oria s/n, 39011 Santander, Spain.


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, CD3εγ and CD3εδ 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 . 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 αβγεδεζζ stoichiometry. The accommodation of a second TCRαβ to fill in the extra volume is discussed.

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