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Pore size matters for potassium channel conductance
Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K(+) channels discriminate K(+) over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport ra...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5037345/ https://www.ncbi.nlm.nih.gov/pubmed/27619418 http://dx.doi.org/10.1085/jgp.201611625 |
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author | Naranjo, David Moldenhauer, Hans Pincuntureo, Matías Díaz-Franulic, Ignacio |
author_facet | Naranjo, David Moldenhauer, Hans Pincuntureo, Matías Díaz-Franulic, Ignacio |
author_sort | Naranjo, David |
collection | PubMed |
description | Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K(+) channels discriminate K(+) over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport rates, covering differences of two orders of magnitude in unitary conductance. The pore domains of large- and small-conductance K(+) channels share a general architectural design comprising a conserved narrow selectivity filter, which forms intimate interactions with permeant ions, flanked by two wider vestibules toward the internal and external openings. In large-conductance K(+) channels, the inner vestibule is wide, whereas in small-conductance channels it is narrow. Here we raise the idea that the physical dimensions of the hydrophobic internal vestibule limit ion transport in K(+) channels, accounting for their diversity in unitary conductance. |
format | Online Article Text |
id | pubmed-5037345 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-50373452017-04-01 Pore size matters for potassium channel conductance Naranjo, David Moldenhauer, Hans Pincuntureo, Matías Díaz-Franulic, Ignacio J Gen Physiol Reviews Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K(+) channels discriminate K(+) over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport rates, covering differences of two orders of magnitude in unitary conductance. The pore domains of large- and small-conductance K(+) channels share a general architectural design comprising a conserved narrow selectivity filter, which forms intimate interactions with permeant ions, flanked by two wider vestibules toward the internal and external openings. In large-conductance K(+) channels, the inner vestibule is wide, whereas in small-conductance channels it is narrow. Here we raise the idea that the physical dimensions of the hydrophobic internal vestibule limit ion transport in K(+) channels, accounting for their diversity in unitary conductance. The Rockefeller University Press 2016-10 /pmc/articles/PMC5037345/ /pubmed/27619418 http://dx.doi.org/10.1085/jgp.201611625 Text en © 2016 Naranjo et al. https://creativecommons.org/licenses/by-nc-sa/3.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ (https://creativecommons.org/licenses/by-nc-sa/3.0/) ). |
spellingShingle | Reviews Naranjo, David Moldenhauer, Hans Pincuntureo, Matías Díaz-Franulic, Ignacio Pore size matters for potassium channel conductance |
title | Pore size matters for potassium channel conductance |
title_full | Pore size matters for potassium channel conductance |
title_fullStr | Pore size matters for potassium channel conductance |
title_full_unstemmed | Pore size matters for potassium channel conductance |
title_short | Pore size matters for potassium channel conductance |
title_sort | pore size matters for potassium channel conductance |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5037345/ https://www.ncbi.nlm.nih.gov/pubmed/27619418 http://dx.doi.org/10.1085/jgp.201611625 |
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