title: High-resolution views of TRPV1 and their implications for the TRP channel superfamily.
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.
authors: Harvard University, Cambridge, MA, USA, hellmich@fas.harvard.edu.
authors: Ute A
authors: UA
authors: Hellmich
authors: Rachelle
authors: R
authors: Gaudet
mesh_terms: D000818:Animals; D020285:Cryoelectron Microscopy; D006801:Humans; D011487:Protein Conformation; D015398:Signal Transduction / Q000502:physiology; D050916:TRPV Cation Channels / Q000737:chemistry* / Q000502:physiology
chemical_list: D050916:TRPV Cation Channels; C494482:TRPV1 protein, human