Keeping calcium in its place: Ca(2+)-ATPase and phospholamban.

Keeping calcium in its place: Ca(2+)-ATPase and phospholamban.
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将钙保持在适当的位置:Ca(2)-ATP 酶和受磷蛋白。

DOI:
10.1016/s0959-440x(97)80121-2
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发表时间:
1997
影响因子:
6.8
通讯作者:
Stokes,DL
Stokes,DL
中科院分区:
生物学2区
文献类型:
--
作者:
Stokes,DL

文献摘要

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相似文献

电子显微镜逐渐揭示了越来越多的关于肌浆网钙泵(Ca2+-ATPase)的结构。最新的结果揭示了 ATP 结合位点,并且正在寻求两种不同的途径来实现更高分辨率的结构。尽管目前受磷蛋白还没有这样的结构,但各种光谱学和定点诱变已经结合起来,产生了一个令人信服的结构模型来调节 Ca2+-ATP 酶。
Electron microscopy is gradually revealing more and more about the structure of the calcium pump from the sarcoplasmic reticulum, Ca2+-ATPase. The most recent result reveals the ATP-binding site, and two different avenues are being pursued towards achieving a higher resolution structure. Although no such structures are currently available for phospholamban, various spectroscopies and site-directed mutagenesis have been combined to produce a compelling structural model for its regulation of Ca2+-ATPase.