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Structure of potassium channels
Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a prokaryotic potassium channel (KcsA, a channel from Streptomyces lividans) was determined, tremendous progress has been made in understanding the me...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Basel
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4565861/ https://www.ncbi.nlm.nih.gov/pubmed/26070303 http://dx.doi.org/10.1007/s00018-015-1948-5 |
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author | Kuang, Qie Purhonen, Pasi Hebert, Hans |
author_facet | Kuang, Qie Purhonen, Pasi Hebert, Hans |
author_sort | Kuang, Qie |
collection | PubMed |
description | Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a prokaryotic potassium channel (KcsA, a channel from Streptomyces lividans) was determined, tremendous progress has been made in understanding the mechanism of potassium channels and channels conducting other ions. In this review, we discuss the structure of various kinds of potassium channels, including the potassium channel with the pore-forming domain only (KcsA), voltage-gated, inwardly rectifying, tandem pore domain, and ligand-gated ones. The general properties shared by all potassium channels are introduced first, followed by specific features in each class. Our purpose is to help readers to grasp the basic concepts, to be familiar with the property of the different domains, and to understand the structure and function of the potassium channels better. |
format | Online Article Text |
id | pubmed-4565861 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Springer Basel |
record_format | MEDLINE/PubMed |
spelling | pubmed-45658612015-09-15 Structure of potassium channels Kuang, Qie Purhonen, Pasi Hebert, Hans Cell Mol Life Sci Review Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a prokaryotic potassium channel (KcsA, a channel from Streptomyces lividans) was determined, tremendous progress has been made in understanding the mechanism of potassium channels and channels conducting other ions. In this review, we discuss the structure of various kinds of potassium channels, including the potassium channel with the pore-forming domain only (KcsA), voltage-gated, inwardly rectifying, tandem pore domain, and ligand-gated ones. The general properties shared by all potassium channels are introduced first, followed by specific features in each class. Our purpose is to help readers to grasp the basic concepts, to be familiar with the property of the different domains, and to understand the structure and function of the potassium channels better. Springer Basel 2015-06-13 2015 /pmc/articles/PMC4565861/ /pubmed/26070303 http://dx.doi.org/10.1007/s00018-015-1948-5 Text en © The Author(s) 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Kuang, Qie Purhonen, Pasi Hebert, Hans Structure of potassium channels |
title | Structure of potassium channels |
title_full | Structure of potassium channels |
title_fullStr | Structure of potassium channels |
title_full_unstemmed | Structure of potassium channels |
title_short | Structure of potassium channels |
title_sort | structure of potassium channels |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4565861/ https://www.ncbi.nlm.nih.gov/pubmed/26070303 http://dx.doi.org/10.1007/s00018-015-1948-5 |
work_keys_str_mv | AT kuangqie structureofpotassiumchannels AT purhonenpasi structureofpotassiumchannels AT heberthans structureofpotassiumchannels |