Journal article
The structural basis for autonomous dimerization of the pre-T-cell antigen receptor
SS Pang, R Berry, Z Chen, L Kjer-Nielsen, MA Perugini, GF King, C Wang, SH Chew, NL La Gruta, NK Williams, T Beddoe, T Tiganis, NP Cowieson, DI Godfrey, AW Purcell, MCJ Wilce, J McCluskey, J Rossjohn
Nature | Published : 2010
DOI: 10.1038/nature09448
Abstract
The pre-T-cell antigen receptor (pre-TCR), expressed by immature thymocytes, has a pivotal role in early T-cell development, including TCR β-selection, survival and proliferation of CD4-CD8- double-negative thymocytes, and subsequent αβ T-cell lineage differentiation1-3. Whereas αβTCR ligation by the peptide-loaded major histocompatibility complex initiates T-cell signalling 4, pre- TCR-induced signalling occurs by means of a ligand-independent dimerization event5. The pre-TCR comprises an invariant α-chain (pre-Ta) that pairs with any TCR β-chain (TCRβ) following successful TCR β-gene rearrangement6. Here we provide the basis of pre-Tα-TCRβ assembly and pre-TCR dimerization. The pre-Tα chai..
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Funding Acknowledgements
We thank S. Turner for discussions; S. Ramarathinam for technical assistance; the staff at the Australian synchrotron (MX and SAXS/WAXS beamlines) and Berkeley Advanced Light Source (SIBYLS beamline) for assistance with data collection; and T. Caradoc-Davies for advice on processing of merohedral twinned X-ray data. This research was supported by grants from the Australian Research Council and the National Health and Medical Research Council of Australia. A.W.P., T.T. and M.C.J.W. are supported by NHMRC Senior Research Fellowships, and D.I.G. is supported by an NHMRC Principal Research Fellowship. M.A.P. is supported by an ARC Future Fellowship and J.R. is supported by an ARC Federation Fellowship.