Apo and InsP₃-bound crystal structures of the ligand-binding domain of an InsP₃ receptor.
Apo and InsP₃-bound crystal structures of the ligand-binding domain of an InsP₃ receptor.
复制标题
DOI:
10.1038/nsmb.2112
复制
发表时间:
2011-09-04
影响因子:
16.8
通讯作者:
中科院分区:
文献类型:
--
作者:
We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate (InsP3) receptor (InsP3R) in its apo and InsP3-bound conformations. Comparison of these two conformations reveals that LBD's first β-trefoil fold (β-TF1) and armadillo repeat fold (ARF) move together as a unit relative to its second β-trefoil fold (β-TF2). Whereas apo-LBD may spontaneously transition between gating conformations, InsP3 binding shifts this equilibrium towards the active state.
登录
查看更多内容
影响因子:
4.8
作者:
Uchida, K;Miyauchi, H;Mikoshiba, K
通讯作者:
Mikoshiba, K
影响因子:
4
作者:
Joseph, SK;Brownell, S;Khan, MT
通讯作者:
Khan, MT
DOI:
10.1006/bbrc.1999.0498
发表时间:
1999-04-21
影响因子:
3.1
作者:
Yoshikawa, F;Uchiyama, T;Mikoshiba, K
通讯作者:
Mikoshiba, K
影响因子:
4.8
作者:
Hamada, K;Terauchi, A;Mikoshiba, K
通讯作者:
Mikoshiba, K
DOI:
10.1073/pnas.88.11.4911
发表时间:
1991-06-01
影响因子:
11.1
作者:
MIYAWAKI, A;FURUICHI, T;MIKOSHIBA, K
通讯作者:
MIKOSHIBA, K