Structure of TRPV1 channel revealed by electron cryomicroscopy

The transient receptor potential (TRP) 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 S...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-05, Vol.105 (21), p.7451-7455
Main Authors: Moiseenkova-Bell, Vera Y, Stanciu, Lia A, Serysheva, Irina I, Tobe, Ben J, Wensel, Theodore G
Format: Article
Language:English
Subjects:
Animals
Ankyrin Repeat
Ankyrins
Biochemistry
Biological Sciences
Cell Membrane - chemistry
Cell membranes
Chromatography
Cryoelectron Microscopy - methods
Crystal structure
Crystallography
Cytoplasm - chemistry
Electronic structure
Electrons
Gene expression
Imaging, Three-Dimensional
Ions
Kv1.2 Potassium Channel - chemistry
Microscopy
Protein Conformation
Proteins
Rats
Receptors
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Signal transduction
TRPC cation channels
TRPV cation channels
TRPV Cation Channels - chemistry
TRPV Cation Channels - genetics
TRPV Cation Channels - isolation & purification
Yeast
Yeasts
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Summary:The transient receptor potential (TRP) 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-Å 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0711835105