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冷冻电镜中的 TRPM7 反射。

TRPM7 reflected in Cryo-EMirror.

机构信息

Walther Straub Institute of Pharmacology and Toxicology, LMU Munich, Germany.

Walther Straub Institute of Pharmacology and Toxicology, LMU Munich, Germany.

出版信息

Cell Calcium. 2018 Dec;76:129-131. doi: 10.1016/j.ceca.2018.11.004. Epub 2018 Nov 15.

Abstract

TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, proliferation and differentiation. Earlier this year, Duan J & co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM). This study tremendously advances our mechanistic understanding of TRPM7 channel function and forms the basis for informed structure-function assessment of this extraordinary protein.

摘要

TRPM7 是一种非典型的离子通道,因为其孔形成部分与蛋白激酶结构域共价连接。通道-激酶 TRPM7 控制着广泛的生物过程,如矿物质稳态、免疫反应、细胞迁移、增殖和分化。今年早些时候,段军及其同事 [1] 通过低温电子显微镜(cryo-EM)解析了三种 TRPM7 结构。这项研究极大地推进了我们对 TRPM7 通道功能的机制理解,并为该非凡蛋白质的结构-功能评估提供了依据。

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