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Journal Article

Structural characterization of the TCR complex by electron microscopy

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Swamy,  Mahima
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Schamel,  Wolfgang A.
Max Planck Society;

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Citation

Arechaga, I., Swamy, M., Abia, D., Schamel, W. A., & Valpuesta, J. M. (2010). Structural characterization of the TCR complex by electron microscopy. International Immunology, 22, 897-903.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-8EA7-2
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, 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 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 αβγεδεζζ stoichiometry. The accommodation of a second TCRαβ to fill in the extra volume is discussed.