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

Author

Listed:
  • 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
    Present address: The Australian Synchrotron, Blackburn Road, Monash, Clayton, Victoria 3168, Australia.)

  • 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)

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.

Suggested Citation

  • 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 , 2010. "The structural basis for autonomous dimerization of the pre-T-cell antigen receptor," Nature, Nature, vol. 467(7317), pages 844-848, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7317:d:10.1038_nature09448
    DOI: 10.1038/nature09448
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