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-Structure paper
タイトル | Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. |
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ジャーナル・号・ページ | J Biol Chem, Vol. 286, Issue 44, Page 38168-38176, Year 2011 |
掲載日 | 2011年11月4日 |
![]() | Teresa L Cvetkov / Kevin W Huynh / Matthew R Cohen / Vera Y Moiseenkova-Bell / ![]() |
PubMed 要旨 | 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. ...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. |
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手法 | EM (単粒子) |
解像度 | 16.0 Å |
構造データ | ![]() EMDB-5334: |
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