A high-resolution crystal structure of the ligand-binding domain of the human nicotinic acetylcholine receptor α subunit, with three point mutations to improve its crystallization, provides both reassurance and exciting new insights.
References
Sine, S.M. & Engel, A.G. Nature 440, 448–455 (2006).
Sixma, T.K. & Smit, A.B. Annu. Rev. Biophys. Biomol. Struct. 32, 311–334 (2003).
Unwin, N. J. Mol. Biol. 346, 967–989 (2005).
Brejc, K. et al. Nature 411, 269–276 (2001).
Dellisanti et al., Nat. Neurosci. 10, 953–962 (2007).
Bouzat, C. et al. Nature 430, 896–900 (2004).
Celie, P.H. et al. Neuron 41, 907–914 (2004).
Hansen, S.B. et al. EMBO J. 24, 3635–3646 (2005).
Bourne, Y., Talley, T.T., Hansen, S.B., Taylor, P. & Marchot, P. EMBO J. 24, 1512–1522 (2005).
Celie, P.H. et al. Nat. Struct. Mol. Biol. 12, 582–588 (2005).
Miyazawa, A., Fujiyoshi, Y. & Unwin, N. Nature 423, 949–955 (2003).
Yao, Y. et al. J. Biol. Chem. 277, 12613–12621 (2002).
Tasneem, A., Iyer, L.M., Jakobsson, E. & Aravind, L. Genome Biol. 6, R4 (2005).
Bocquet, N. et al. Nature 445, 116–119 (2007).
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Sixma, T. Nicotinic receptor structure emerging slowly. Nat Neurosci 10, 937–938 (2007). https://doi.org/10.1038/nn0807-937
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DOI: https://doi.org/10.1038/nn0807-937
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