Structure of the mouse TRPC4 ion channel.
Structure of the mouse TRPC4 ion channel.
复制标题
小鼠TRPC4离子通道的结构
DOI:
10.1038/s41467-018-05247-9
复制
发表时间:
2018-08-06
影响因子:
16.6
通讯作者:
Zhang J
中科院分区:
文献类型:
--
作者:
Duan J;Li J;Zeng B;Chen GL;Peng X;Zhang Y;Wang J;Clapham DE;Li Z;Zhang J
Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar and primary ciliary signaling. Here we report a cryo-electron microscopy (cryo-EM) structure of TRPC4 in its unliganded (apo) state to an overall resolution of 3.3 Å. The structure reveals a unique architecture with a long pore loop stabilized by a disulfide bond. Beyond the shared tetrameric six-transmembrane fold, the TRPC4 structure deviates from other TRP channels with a unique cytosolic domain. This unique cytosolic N-terminal domain forms extensive aromatic contacts with the TRP and the C-terminal domains. The comparison of our structure with other known TRP structures provides molecular insights into TRPC4 ion selectivity and extends our knowledge of the diversity and evolution of the TRP channels.
登录
查看更多内容
影响因子:
48
作者:
Kucukelbir, Alp;Sigworth, Fred J.;Tagare, Hemant D.
通讯作者:
Tagare, Hemant D.
影响因子:
4.8
作者:
Beck, Andreas;Speicher, Tilman;Flockerzi, Veit
通讯作者:
Flockerzi, Veit
影响因子:
4.5
作者:
Hong, Chansik;Kwak, Misun;So, Insuk
通讯作者:
So, Insuk
DOI:
10.1107/s0907444909052925
发表时间:
2010-02
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者:
Zwart PH
影响因子:
64.8
作者:
Paulsen, Candice E.;Armache, Jean-Paul;Gao, Yuan;Cheng, Yifan;Julius, David
通讯作者:
Julius, David