Structural Basis for Gating and Activation of RyR1.
Structural Basis for Gating and Activation of RyR1.
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DOI:
10.1016/j.cell.2016.08.075
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发表时间:
2016-09-22
期刊:
影响因子:
64.5
通讯作者:
Frank, Joachim
中科院分区:
文献类型:
--
作者:
des Georges, Amedee;Clarke, Oliver B.;Zalk, Ran;Yuan, Qi;Condon, Kendall J.;Grassucci, Robert A.;Hendrickson, Wayne A.;Marks, Andrew R.;Frank, Joachim
The type-1 ryanodine receptor (RyR1) is an intracellular calcium (Ca2+) release channel required for skeletal muscle contraction. Here we present cryo-EM reconstructions of RyR1 in multiple functional states revealing the structural basis of channel gating and ligand-dependent activation. Binding sites for the channel activators Ca2+, ATP and caffeine were identified at interdomain interfaces of the C-terminal domain. Either ATP or Ca2+ alone induce conformational changes in the cytoplasmic assembly (‘priming’), without pore dilation. In contrast, in the presence of all three activating ligands, high-resolution reconstructions of open and closed states of RyR1 were obtained from the same sample, enabling analyses of conformational changes associated with gating. Gating involves global conformational changes in the cytosolic assembly accompanied by local changes in the transmembrane domain, which include bending of the S6 transmembrane segment and consequent pore dilation, displacement and deformation of the S4-S5 linker, and conformational changes in the pseudo-voltage-sensor domain.
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影响因子:
48
作者:
Barad BA;Echols N;Wang RY;Cheng Y;DiMaio F;Adams PD;Fraser JS
通讯作者:
Fraser JS
影响因子:
64.8
作者:
Fan G;Baker ML;Wang Z;Baker MR;Sinyagovskiy PA;Chiu W;Ludtke SJ;Serysheva II
通讯作者:
Serysheva II
DOI:
10.1073/pnas.012688999
发表时间:
2002-12-24
影响因子:
11.1
作者:
Du, GG;Sandhu, B;MacLennan, DH
通讯作者:
MacLennan, DH
影响因子:
3.9
作者:
CARROLL, S;SKARMETA, JG;INESI, G
通讯作者:
INESI, G
影响因子:
64.5
作者:
BRILLANTES, AMB;ONDRIAS, K;MARKS, AR
通讯作者:
MARKS, AR