生物物理学
钙
化学
细胞质
机制(生物学)
跨膜蛋白
低温电子显微
结合位点
蛋白质结构
钙结合蛋白
细胞生物学
纳米技术
生物化学
生物
材料科学
受体
物理
有机化学
量子力学
作者
Wang Ji,Donghong Shi,Sai Shi,Xiao Yang,Yafei Chen,Hailong An,Chunli Pang
出处
期刊:Protein and Peptide Letters
[Bentham Science]
日期:2021-12-01
卷期号:28 (12): 1338-1348
被引量:2
标识
DOI:10.2174/0929866528666211105112131
摘要
TMEM16A mediates the calcium-activated transmembrane flow of chloride ions and a variety of physiological functions. The binding of cytoplasmic calcium ions of TMEM16A and the consequent conformational changes of it are the key issues to explore the structure-function relationship. In recent years, researchers have explored this issue through electrophysiological experiments, structure resolving, molecular dynamic simulation, and other methods. The structures of TMEM16 family members determined by cryo-Electron microscopy (cryo-EM) and X-ray crystallization provide the primary basis for the investigation of the molecular mechanism of TMEM16A. However, the binding and activation mechanism of calcium ions in TMEM16A are still unclear and controversial. This mini-review discusses four Ca2+ sensing sites of TMEM16A and analyzes activation properties of TMEM16A by them, which will help understand the structure-function relationship of TMEM16A and throw light on the molecular design targeting the TMEM16A channel.
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