Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 21, Pages 7451-7455Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0711835105
Keywords
cryoelectron microscopy; ion channels; TRP channels
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Funding
- NCRR NIH HHS [P41-RR02250, P41 RR002250] Funding Source: Medline
- NEI NIH HHS [R01-EY07981, R01 EY007981] Funding Source: Medline
- NIDDK NIH HHS [T90-DK071505, R90 DK071505] Funding Source: Medline
- NIGMS NIH HHS [P01-GM99116, R01-GM072804, R01 GM072804] Funding Source: Medline
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The transient receptor potential (TRIP) family of ion channels participate in many signaling pathways. TRPV1 functions as a molecular integrator of noxious stimuli, including heat, low pH, and chemical ligands. Here, we report the 3D structure of full-length rat TRPV1 channel expressed in the yeast Saccharomyces cerevisiae and purified by immunoaffinity chromatography. We demonstrate that the recombinant purified TRPV1 channel retains its structural and functional integrity and is suitable for structural analysis. The 19-angstrom structure of TRPV1 determined by using single-particle electron cryomicroscopy exhibits fourfold symmetry and comprises two distinct regions: a large open basket-like domain, likely corresponding to the cytoplasmic N- and C-terminal portions, and a more compact domain, corresponding to the transmembrane portion. The assignment of transmembrane and cytoplasmic regions was supported by fitting crystal structures of the structurally homologous Kv1.2 channel and isolated TRPV1 ankyrin repeats into the TRPV1 structure.
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