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兰尼碱受体1结构及其通道门控机制的研究进展
顾嘉伟1,邓宇晨2,徐拯3,肖良4*
0
(1. 第二军医大学临床医学专业学员十一队, 上海 200433;
2. 第二军医大学海军临床医学专业学员三队, 上海 200433;
3. 第二军医大学科研部, 上海 200433;
4. 第二军医大学海军医学系海洋生物技术教研室, 上海 200433
*通信作者)
摘要:
兰尼碱受体(ryanodine receptor, RyR)是位于肌浆网膜上的细胞内Ca2+释放通道,在骨骼肌和心肌兴奋收缩偶联等生理过程中发挥重要作用。随着单粒子冷冻电镜技术的应用以及数据分析能力的提高,近期来自中国、美国以及德国的3个课题组分别获得了整体分辨率为3.8Å (1Å=10-10m)、4.8Å和6.1Å的高清晰RyR1结构图片,相关研究同时发表于2015年第1期的Nature上,是近年来RyR结构及其门控研究的重要进展。RyR1为相对分子质量>2200000的同源四聚体离子通道,主要包括由NTD、SPRY、P1、P2、B-sol以及C-sol等结构域组成的胞质区和由S1~S6、VSL以及CTD等结构域组成的通道区。Ca2+作为RyR1门控的主要影响因子,能够与胞质区EF-hand亚结构域结合,引起通道构象的变化并最终导致通道的开放。
关键词:  兰尼碱受体    通道  冷冻电镜  结构
DOI:10.16781/j.0258-879x.2016.07.0873
投稿时间:2016-03-15修订日期:2016-06-07
基金项目:国家自然科学基金面上项目(81470518),2015年度第二军医大学大学生创新基金面上项目(MS2015014,MS2015028).
Ryanodine receptor 1 and its potential gating mechanism: recent progress
GU Jia-wei1,DENG Yu-chen2,XU Zheng3,XIAO Liang4*
(1. No. 11 Student Team, Clinical Medicine, Second Military Medical University, Shanghai 200433, China;
2. No.;
3 Student Team, Naval Clinical Medicine, Second Military Medical University, Shanghai 200433, China;
3. Division of Scientific Research Administration, Second Military Medical University, Shanghai 200433, China;
4. Department of Marine Biotechnology, Faculty of Naval Medicine, Second Military Medical University, Shanghai 200433, China
* Corresponding author)
Abstract:
The ryanodine receptors (RyRs) are intracellular Ca2+ releasing channels on the sarcoplasmic reticulum membrane and play a pivotal role in the excitation-contraction coupling of skeletal and cardiac muscles as well as other physiological processes. With the recent development of Cryo-EM and the improvement of data analysis technique, scientists from China, the United States and Germany have acquired high-quality RyR1 images at the total resolutions of 3.8 Å (1 Å=10-10 m), 4.8 Å and 6.1 Å, respectively, which have been published in the same issue of Nature in 2015. RyR1s are homotetrameric complexes with a molecular mass of more than 2200000, mainly containing a cytoplasmic region composed of NTD, SPRY, P1, P2, B-sol and C-sol domains and a channel region composed of S1-S6, VSL and CTD domains. As the most common factor affecting the condition of RyR1, Ca2+ is able to bind the EF-hand subdomain in the cytoplasmic region, which further causes the conformational change and finally leads to the channel opening.
Key words:  ryanodine receptor  calcium  channel  cryo-electronic microscopy  structure