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学科主题: 基础医学
题名:
The structural basis of Ca2+ transport by the Ca2+-ATPase from skeletal sarcoplasmic reticulum
作者: Wei, RS; Wang, PR; Yin, CC
关键词: Ca2+-pump (Ca2+-ATPase) ; crystal structure ; conformational change
刊名: PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
发表日期: 2006-03-01
卷: 33, 期:3, 页:210-220
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]: Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]: P-TYPE ATPASES ; CALCIUM-PUMP ; CRYSTAL-STRUCTURE ; ION-TRANSPORT ; MECHANISM ; BINDING ; OCCLUSION ; FORMS ; DISSOCIATION ; ACTIVATION
英文摘要:

The Ca2+-ATPase of sarcoplasmic reticulum is a Ca2+ pump that plays a key role in regulating cytosol calcium concentration in muscle cells. It undergoes a sequential conformational transition during the transport process. According to the classical E1/E2 theory, in the E1 state the binding sites have high affinity and open to the cytoplasm, whereas in the E2 state the binding sites have low affinity and face the luminal side. Crystal structures of several states during the reaction cycle of Ca2+-ATPase have been solved recently, including a Ca2+-bound form (E1-2Ca(2+)), a Ca2+-unbound form stabilized by a potent inhibitor thapsigargin (TG) (E2-TG), an ATP-bound form (E1-ATP), an E1-P-ADP state, and an E2-Pi state. The details of these crystal structures and the relationship between structure and function of Ca2+-ATPase during reaction cycle were summarized, and the issues to be addressed in future research were raised.

语种: 中文
WOS记录号: WOS:000236134000002
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/51055
Appears in Collections:基础医学院_生物物理学系_期刊论文

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作者单位: Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100083, Peoples R China

Recommended Citation:
Wei, RS,Wang, PR,Yin, CC. The structural basis of Ca2+ transport by the Ca2+-ATPase from skeletal sarcoplasmic reticulum[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2006,33(3):210-220.
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