肌浆网Ca2+-ATP酶的结构
The structure of the Ca2+-ATPase of sarcoplasmic reticulum.
作者信息
Martonosi Anthony N, Pikula Slawomir
机构信息
Upstate Medical University, College of Graduate Studies, State University of New York, Syracuse, NY, U.S.A.
出版信息
Acta Biochim Pol. 2003;50(2):337-65.
In this article the morphology of sarcoplasmic reticulum, classification of Ca(2+)-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca(2+)-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca(2+)-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca(2+)-ATPase to the sarcoplasmic reticulum is discussed.
在本文中，我们将综述肌浆网的形态学、该膜系统中存在的Ca(2+)-ATP酶（SERCA）同工酶的分类及其拓扑结构。重点是通过电子和X射线晶体学、肌浆网多层膜中Ca(2+)-ATP酶轮廓结构的层状X射线和中子衍射分析所确定的Ca(2+)-ATP酶的结构和相互作用。此外，还将讨论Ca(2+)-ATP酶在肌浆网上的靶向作用。
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