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Ctr1铜转运蛋白的结构揭示了新的架构。

Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture.

作者信息

Nose Yasuhiro, Rees Erin M, Thiele Dennis J

机构信息

Department of Pharmacology and Cancer Biology, Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Research Drive-LSRC C351, Durham, NC 27710-3813, USA.

出版信息

Trends Biochem Sci. 2006 Nov;31(11):604-7. doi: 10.1016/j.tibs.2006.09.003. Epub 2006 Sep 18.

Abstract

Copper is essential for biological processes such as free radical detoxification, mitochondrial respiration and iron metabolism. A central player in copper homeostasis is the high-affinity integral plasma membrane copper transporter Ctr1. However, the precise mechanisms by which Ctr1 functions are not known. Here, we highlight an important breakthrough in our understanding of how Ctr1 facilitates Cu(I) movement across membranes: the publication of structural details for human Ctr1 obtained from 2D crystallography and electron microscopy.

摘要

铜对于诸如自由基解毒、线粒体呼吸和铁代谢等生物过程至关重要。铜稳态的核心参与者是高亲和力的整合质膜铜转运蛋白Ctr1。然而,Ctr1发挥功能的确切机制尚不清楚。在这里,我们重点介绍了我们对Ctr1如何促进Cu(I)跨膜移动的理解方面的一项重要突破:通过二维晶体学和电子显微镜获得的人类Ctr1结构细节的发表。

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