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.
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DOI:
10.1038/nsmb.2112
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发表时间:
2011-09-04
影响因子:
16.8
通讯作者:
--
中科院分区:
生物学1区
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本文报道了大鼠肌醇1,4,5-三磷酸(InsP3)受体(InsP3R)的配体结合域(LBD)在其apo构象和InsP3结合构象中的晶体结构。对这两种构象的比较表明,LBD的第一个β-三叶折叠(β-Tf1)和犰螂重复折叠(ARF)作为一个单位相对于第二个β-三叶折叠(β-Tf2)一起移动。虽然apo-LBD可以自发地在门控构象之间转换,但InsP3结合使这种平衡向活性状态移动。
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.
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