The structural basis for autonomous dimerization of the pre-T-cell antigen receptor

Siew Siew Pang, Richard Berry, Zhenjun Chen, Lars Kjer-Nielsen, Matthew A. Perugini, Glenn F. King, Christina Wang, Sock Hui Chew, Nicole L. La Gruta, Neal K. Williams, Travis Beddoe, Tony Tiganis, Nathan P. Cowieson, Dale I. Godfrey, Anthony W. Purcell, Matthew C. J. Wilce, James McCluskey () and Jamie Rossjohn ()
Additional contact information
Siew Siew Pang: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Richard Berry: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Zhenjun Chen: University of Melbourne
Lars Kjer-Nielsen: University of Melbourne
Matthew A. Perugini: University of Melbourne
Glenn F. King: Institute for Molecular Bioscience, The University of Queensland
Christina Wang: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Sock Hui Chew: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Nicole L. La Gruta: University of Melbourne
Neal K. Williams: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Travis Beddoe: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Tony Tiganis: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Nathan P. Cowieson: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
Dale I. Godfrey: University of Melbourne
Anthony W. Purcell: University of Melbourne
Matthew C. J. Wilce: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University
James McCluskey: University of Melbourne
Jamie Rossjohn: The Protein Crystallography Unit, School of Biomedical Sciences, Monash University

Nature, 2010, vol. 467, issue 7317, 844-848

Abstract: Pre-T-cell receptor structure The pre-T-cell antigen receptor (pre-TCR) plays an important part in adaptive immunity by mediating early T-cell development and differentiation. The structure of pre-TCR and the pre-TCR dimer have now been determined, revealing how the head-to-tail dimeric arrangement allows the interaction of the invariant α (pre-Tα) domain with any variable (V) β domain, and provides the basis for ligand-independent signalling.

Date: 2010
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DOI: 10.1038/nature09448

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