Ryanodine receptor assembly: A novel systems biology approach to 3D mapping
Ryanodine receptor assembly: A novel systems biology approach to 3D mapping
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DOI：
10.1016/j.pbiomolbio.2010.09.021
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发表时间：
2011-05-01
影响因子：
3.8
通讯作者：
Kim, Do Han
中科院分区：
文献类型：
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作者：
Song, Dong Woo;Lee, Jung-Gyu;Kim, Do Han
Ryanodine受体（RyRs）是细胞内Ca2+释放通道（CRCs），在细胞Ca2+信号传导中起关键作用。在横纹肌中，ryr介导的Ca2+从肌浆网（SR）释放诱导细胞质Ca2+浓度升高和随后的肌肉收缩。来自各种来源的证据表明，相同四聚体构象的RyRs在中央孔和大细胞质域形成了一个大电导的Ca2+可渗透通道。ryr与各种细胞质和管腔蛋白形成一个大的组装体。关于RyRs的功能和相关蛋白的调控已经发表了许多论文，但尚未详细讨论其组装的三维（3D）结构。在本文中，我们试图通过考虑已发表的cryo-EM数据，可用的x射线晶体学信息和分子建模方法，建立ryr组装的3d地图。(C) 2010 Elsevier Ltd.版权所有。
Ryanodine receptors (RyRs) are intracellular Ca2+ release channels (CRCs) that play a pivotal role in cellular Ca2+ signaling. In striated muscles, RyR-mediated Ca2+ release from the sarcoplasmic reticulum (SR) induces elevation of cytosolic Ca2+ concentration and subsequent muscle contraction. Evidence from various sources suggests that RyRs in homo-tetrameric conformation form a large conductance Ca2+ permeable channel in the central pore and large cytoplasmic domains. RyRs form a large assembly with various cytosolic and luminal proteins. A number of papers have been published concerning the functions of RyRs and the regulation of the associated proteins, but the three dimensional (3D) structure of the assembly has not been addressed in detail. In this paper, we have attempted to establish a 3D-map for the assembly of RyRs by considering published cryo-EM data, available X-ray crystallographic information and molecular modeling methods. (C) 2010 Elsevier Ltd. All rights reserved.