6CUD

Structure of the human TRPC3 in a lipid-occupied, closed state

6CUD の概要

• エントリーDOI: 10.2210/pdb6cud/pdb
• EMDBエントリー: 7620
• 分子名称: Short transient receptor potential channel 3, (2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl hexanoate, (2R)-3-hydroxypropane-1,2-diyl dihexanoate, ... (4 entities in total)
• 機能のキーワード: canonical transient receptor potential 3 (trpc3) lipid-sensitive non-selective cation channel, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 374449.03

構造登録者

Lu, W.,Du, J.,Fan, C.,Choi, W. (登録日: 2018-03-25, 公開日: 2018-05-16, 最終更新日: 2024-10-30)

主引用文献

Fan, C.,Choi, W.,Sun, W.,Du, J.,Lu, W.
Structure of the human lipid-gated cation channel TRPC3.
Elife, 7:-, 2018

PubMed 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.

PubMed: 29726814
DOI: 10.7554/eLife.36852

実験手法

ELECTRON MICROSCOPY (3.3 Å)