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-Structure paper
タイトル | Structure of the human lipid-gated cation channel TRPC3. |
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ジャーナル・号・ページ | Elife, Vol. 7, Year 2018 |
掲載日 | 2018年5月4日 |
著者 | Chen Fan / Wooyoung Choi / Weinan Sun / Juan Du / Wei Lü / |
PubMed 要旨 | The TRPC channels are crucially involved in store-operated calcium entry and calcium homeostasis, and they are implicated in human diseases such as neurodegenerative disease, cardiac hypertrophy, and ...The TRPC channels are crucially involved in store-operated calcium entry and calcium homeostasis, and they are implicated in human diseases such as neurodegenerative disease, cardiac hypertrophy, and spinocerebellar ataxia. We present a structure of the full-length human TRPC3, a lipid-gated TRPC member, in a lipid-occupied, closed state at 3.3 Angstrom. TRPC3 has four elbow-like membrane reentrant helices prior to the first transmembrane helix. The TRP helix is perpendicular to, and thus disengaged from, the pore-lining S6, suggesting a different gating mechanism from other TRP subfamily channels. The third transmembrane helix S3 is remarkably long, shaping a unique transmembrane domain, and constituting an extracellular domain that may serve as a sensor of external stimuli. We identified two lipid-binding sites, one being sandwiched between the pre-S1 elbow and the S4-S5 linker, and the other being close to the ion-conducting pore, where the conserved LWF motif of the TRPC family is located. |
リンク | Elife / PubMed:29726814 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 Å |
構造データ | |
化合物 | ChemComp-6OE: ChemComp-FGJ: ChemComp-NAG: |
由来 |
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キーワード | MEMBRANE PROTEIN / Canonical transient receptor potential 3 (TRPC3) lipid-sensitive non-selective cation channel |