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eLife, May 04 2018, 7 e36852 | https://doi.org/10.7554/eLife.36852 Structure of the human lipid-gated cation channel TRPC3

Chen Fan ^{1 †}, Wooyoung Choi ^{1 †}, Weinan Sun 2, Juan Du^{1 *}, Wei Lü ^{1 *}

¹Van Andel Institute, Grand Rapids, United States.
²Vollum Institute, Portland, United States.

^†These authors contributed equally
^*Corresponding authors: correspondence to Juan Du or Wei Lü

Abstract

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.

논문정보

형식Research article
게재일2018년 05월 (BRIC 등록일 2025-02-28)
연구진국외 연구진
분야
피인용횟수120회 이상 인용된 논문

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