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TitleMolecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy.
Journal, issue, pagesJ Biol Chem, Vol. 286, Issue 44, Page 38168-38176, Year 2011
Publish dateNov 4, 2011
AuthorsTeresa L Cvetkov / Kevin W Huynh / Matthew R Cohen / Vera Y Moiseenkova-Bell /
PubMed AbstractTransient receptor potential ankyrin 1 (TRPA1) is a non-selective ion channel, which is expressed in nociceptor sensory neurons and transduces chemical, inflammatory, and neuropathic pain signals. ...Transient receptor potential ankyrin 1 (TRPA1) is a non-selective ion channel, which is expressed in nociceptor sensory neurons and transduces chemical, inflammatory, and neuropathic pain signals. Numerous non-reactive compounds and electrophilic compounds, such as endogenous inflammatory mediators and exogenous pungent chemicals, can activate TRPA1. Here we report a 16-Å resolution structure of purified, functional, amphipol-stabilized TRPA1 analyzed by single-particle EM. Molecular models of the N and C termini of the channel were generated using the I-TASSER protein structure prediction server and docked into the EM density to provide insight into the TRPA1 subunit organization. This structural analysis suggests a location for critical N-terminal cysteine residues involved in electrophilic activation at the interface between neighboring subunits. Our results indicate that covalent modifications within this pocket may alter interactions between subunits and promote conformational changes that lead to channel activation.
External linksJ Biol Chem / PubMed:21908607 / PubMed Central
MethodsEM (single particle)
Resolution16.0 Å
Structure data

EMDB-5334:
TRPA1 channel structure at 16A resolution
Method: EM (single particle) / Resolution: 16.0 Å

Source
  • Mus musculus (house mouse)

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