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Recent progress in structural studies on TMEM16A channel

The calcium-activated chloride channel, also known as TMEM16A, shows both calcium and membrane potential dependent activation. The channel is expressed broadly and contributes to a variety of physiological processes, and it is expected to be a target for the treatment of diseases such as hypertensio...

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Detalles Bibliográficos
Autores principales: Shi, Sai, Pang, Chunli, Guo, Shuai, Chen, Yafei, Ma, Biao, Qu, Chang, Ji, Qiushuang, An, Hailong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7118279/
https://www.ncbi.nlm.nih.gov/pubmed/32257055
http://dx.doi.org/10.1016/j.csbj.2020.03.015
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author Shi, Sai
Pang, Chunli
Guo, Shuai
Chen, Yafei
Ma, Biao
Qu, Chang
Ji, Qiushuang
An, Hailong
author_facet Shi, Sai
Pang, Chunli
Guo, Shuai
Chen, Yafei
Ma, Biao
Qu, Chang
Ji, Qiushuang
An, Hailong
author_sort Shi, Sai
collection PubMed
description The calcium-activated chloride channel, also known as TMEM16A, shows both calcium and membrane potential dependent activation. The channel is expressed broadly and contributes to a variety of physiological processes, and it is expected to be a target for the treatment of diseases such as hypertension, pain, cystic fibrosis and lung cancer. A thorough understanding of the structural characteristics of TMEM16A is important to reveal its physiological and pathological roles. Recent studies have released several Cryo-EM structures of the channel, revealed the structural basis and mechanism of the gating of the channel. This review focused on the understandings of the structural basis and molecular mechanism of the gating and permeation of TMEM16A channel, which will provide important basis for the development of drugs targeting TMEM16A.
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spelling pubmed-71182792020-04-06 Recent progress in structural studies on TMEM16A channel Shi, Sai Pang, Chunli Guo, Shuai Chen, Yafei Ma, Biao Qu, Chang Ji, Qiushuang An, Hailong Comput Struct Biotechnol J Review Article The calcium-activated chloride channel, also known as TMEM16A, shows both calcium and membrane potential dependent activation. The channel is expressed broadly and contributes to a variety of physiological processes, and it is expected to be a target for the treatment of diseases such as hypertension, pain, cystic fibrosis and lung cancer. A thorough understanding of the structural characteristics of TMEM16A is important to reveal its physiological and pathological roles. Recent studies have released several Cryo-EM structures of the channel, revealed the structural basis and mechanism of the gating of the channel. This review focused on the understandings of the structural basis and molecular mechanism of the gating and permeation of TMEM16A channel, which will provide important basis for the development of drugs targeting TMEM16A. Research Network of Computational and Structural Biotechnology 2020-03-21 /pmc/articles/PMC7118279/ /pubmed/32257055 http://dx.doi.org/10.1016/j.csbj.2020.03.015 Text en © 2020 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review Article
Shi, Sai
Pang, Chunli
Guo, Shuai
Chen, Yafei
Ma, Biao
Qu, Chang
Ji, Qiushuang
An, Hailong
Recent progress in structural studies on TMEM16A channel
title Recent progress in structural studies on TMEM16A channel
title_full Recent progress in structural studies on TMEM16A channel
title_fullStr Recent progress in structural studies on TMEM16A channel
title_full_unstemmed Recent progress in structural studies on TMEM16A channel
title_short Recent progress in structural studies on TMEM16A channel
title_sort recent progress in structural studies on tmem16a channel
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7118279/
https://www.ncbi.nlm.nih.gov/pubmed/32257055
http://dx.doi.org/10.1016/j.csbj.2020.03.015
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