STRUCTURE-FUNCTION-RELATIONSHIPS OF THE MOUSE INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR
STRUCTURE-FUNCTION-RELATIONSHIPS OF THE MOUSE INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR
复制标题
DOI：
10.1073/pnas.88.11.4911
复制
发表时间：
1991-06-01
影响因子：
11.1
通讯作者：
MIKOSHIBA, K
中科院分区：
文献类型：
--
作者：
MIYAWAKI, A;FURUICHI, T;MIKOSHIBA, K
肌醇1,4,5-三磷酸（InsP3）受体的同四聚体复合物响应于InsP3分子表现出Ca2+释放活性。通过分析NG108-15细胞中表达的一系列内部缺失或c端截断突变蛋白，研究了小鼠小脑InsP3受体的结构-功能关系。在InsP3受体的大细胞质部分中，约有650个n端氨基酸在小鼠和果蝇之间高度保守，该区域具有InsP3结合的关键序列，可能形成三维限制性结合位点。每个InsP3受体亚基的n端区域也结合一个InsP3分子。交联实验表明，InsP3受体在跨膜结构域和/或连续的C端是分子间结合的。受体亚基与InsP3之间的相互作用可能导致四聚体复合物的构象改变，导致Ca2+通道的打开。
The homotetrameric complex of inositol 1,4,5-trisphosphate (InsP3) receptors displays a Ca2+ release activity in response to InsP3 molecules. Structure-function relationships of the mouse cerebellar InsP3 receptor have been studied by analyses of a series of internal deletion or C-terminal truncation mutant proteins expressed in NG108-15 cells. Within the large cytoplasmic portion of the InsP3 receptor, almost-equal-to 650 N-terminal amino acids are highly conserved between mouse and Drosophila, and this region has the critical sequences for InsP3 binding that probably form the three-dimensionally restricted binding site. The N-terminal region of each InsP3 receptor subunit also binds one InsP3 molecule. Cross-linking experiments have revealed that InsP3 receptors are intermolecularly associated at the transmembrane domains and/or the successive C termini. The interaction between the receptor subunit and InsP3 may cause a conformational change in the tetrameric complex, resulting in the opening of Ca2+ channels.