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Abstract
The first high-resolution structures of a near-full-length TRP channel were recently described, structures of the noxious heat receptor TRPV1 in the absence or presence of vanilloid agonists and a spider toxin. Here we briefly review the salient features, including the overall architecture, agonist binding sites, and conformational changes related to channel pore gating. We also discuss some of the structures' implications for the TRP channel family and a few of the many questions still left unanswered.
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