Apo and InsP3-bound crystal structures of the ligand-binding domain of an InsP3 receptor

被引：70

作者：

Lin, Chun-Chi ^{[1
]}

Baek, Kyuwon ^{[1
]}

Lu, Zhe ^{[1
]}

机构：

[1] Univ Penn, Howard Hughes Med Inst, Dept Physiol, Perelman Sch Med, Philadelphia, PA 19104 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 10期

关键词：

INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; 3-DIMENSIONAL STRUCTURE; SITE;

D O I：

10.1038/nsmb.2112

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate receptor (InsP(3)R) in its apo and InsP(3)-bound conformations. Comparison of these two conformations reveals that LBD's first beta-trefoil fold (beta-TF1) and armadillo repeat fold (ARF) move together as a unit relative to its second beta-trefoil fold (beta-TF2). Whereas apo LBD may spontaneously transition between gating conformations, InsP(3) binding shifts this equilibrium toward the active state.

引用

页码：1172 / 1174

页数：3

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