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Nicotinic receptor structure emerging slowly

Nature Neuroscience volume 10, pages 937–938 (2007)Cite this article

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.

For the longest time, the nicotinic acetylcholine receptor (nAChR) has served as a playground for the neurobiology community, allowing relatively early and easy testing of concepts in neurotransmission1,2. Nicotinic receptors provided the early work on ion channels, the testing ground for electrophysiology, the arena for sequencing, a test site for neurotoxins, the first electron microscopy images and an opportunity for cysteine-scanning mutagenesis. However, in the realm of high-resolution structures, the nicotinic receptors have lagged behind.

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Figure 1: The α subunit of the nAChR ligand binding domain has been resolved at high resolution.
Figure 2: Features of the new nAChR α subunit structure.

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Authors and Affiliations

  1. Titia K. Sixma is at the Department of Molecular Carcinogenesis, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands. t.sixma@nki.nl,

    Titia K Sixma

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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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