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Edited by Clara Franzini-Armstrong, University of Pennsylvania School of Medicine, Philadelphia, PA, and approved March 6, 2008 (received for review December 16, 2007)
Abstract
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.
Footnotes
- ‡To whom correspondence should be addressed at: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. E-mail: twensel{at}bcm.tmc.edu
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Author contributions: V.Y.M.-B. and T.G.W. designed research; V.Y.M.-B. and L.A.S. performed research; V.Y.M.-B. and B.J.T. contributed new reagents/analytic tools; V.Y.M.-B., L.A.S., I.I.S., and T.G.W. analyzed data; and V.Y.M.-B., I.I.S., and T.G.W. wrote the paper.
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The authors declare no conflict of interest.
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This article is a PNAS Direct Submission.
- © 2008 by The National Academy of Sciences of the USA
Structure of TRPV1 channel revealed by electron cryomicroscopy
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