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Structural biology

Pain-sensing TRPA1 channel resolved

Nature volume 520, pages 439–441 (2015)Cite this article

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The TRPA1 ion channel activates pain pathways in response to noxious compounds. The structure of TRPA1 has now been solved, providing insight into how it functions. See Article p.511

Rooted in place, many plants resort to chemical warfare to survive predation by bacteria, fungi, insects and mammalian herbivores. They produce pungent natural chemicals, such as capsaicin, which makes chilli peppers 'hot', and the thiosulfinates that make onion chopping a tear-jerker. Reactive chemicals in onions, wasabi and related spices activate the ion channel TRPA1, a relative of the capsaicin receptor TRPV1. On page 511 of this issue, Paulsen et al.1 follow up their description of TRPV1 (refs 2, 3). Using electron cryo-microscopy techniques, they define the full-length, single-particle structure of TRPA1 to around 4 ångströms, a level of resolution that reveals its general features.

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Figure 1: The structure of TRPA1.

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References

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Authors and Affiliations

  1. Department of Cardiology, and the Department of Neurobiology, David E. Clapham is at the Howard Hughes Medical Institute, Boston Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.,

    David E. Clapham

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  1. David E. Clapham
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Correspondence to David E. Clapham.

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Clapham, D. Pain-sensing TRPA1 channel resolved. Nature 520, 439–441 (2015). https://doi.org/10.1038/nature14383

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