CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1

Na+-coupled acid-base membrane transport proteins regulate blood pressure, ion homeostasis and acid-base chemistry. Here the authors present the 3.9 Å resolution cryoEM structure of the sodium-bicarbonate cotransporter NBCe1 and characterize its ion coordination site and ion accessibility pathway wi...

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Autores principales: Kevin W. Huynh, Jiansen Jiang, Natalia Abuladze, Kirill Tsirulnikov, Liyo Kao, Xuesi Shao, Debra Newman, Rustam Azimov, Alexander Pushkin, Z. Hong Zhou, Ira Kurtz
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/8364ae1d1dec4883ada874ff703311fb
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spelling oai:doaj.org-article:8364ae1d1dec4883ada874ff703311fb2021-12-02T17:32:46ZCryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe110.1038/s41467-018-03271-32041-1723https://doaj.org/article/8364ae1d1dec4883ada874ff703311fb2018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03271-3https://doaj.org/toc/2041-1723Na+-coupled acid-base membrane transport proteins regulate blood pressure, ion homeostasis and acid-base chemistry. Here the authors present the 3.9 Å resolution cryoEM structure of the sodium-bicarbonate cotransporter NBCe1 and characterize its ion coordination site and ion accessibility pathway with mutagenesis experiments.Kevin W. HuynhJiansen JiangNatalia AbuladzeKirill TsirulnikovLiyo KaoXuesi ShaoDebra NewmanRustam AzimovAlexander PushkinZ. Hong ZhouIra KurtzNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Kevin W. Huynh
Jiansen Jiang
Natalia Abuladze
Kirill Tsirulnikov
Liyo Kao
Xuesi Shao
Debra Newman
Rustam Azimov
Alexander Pushkin
Z. Hong Zhou
Ira Kurtz
CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
description Na+-coupled acid-base membrane transport proteins regulate blood pressure, ion homeostasis and acid-base chemistry. Here the authors present the 3.9 Å resolution cryoEM structure of the sodium-bicarbonate cotransporter NBCe1 and characterize its ion coordination site and ion accessibility pathway with mutagenesis experiments.
format article
author Kevin W. Huynh
Jiansen Jiang
Natalia Abuladze
Kirill Tsirulnikov
Liyo Kao
Xuesi Shao
Debra Newman
Rustam Azimov
Alexander Pushkin
Z. Hong Zhou
Ira Kurtz
author_facet Kevin W. Huynh
Jiansen Jiang
Natalia Abuladze
Kirill Tsirulnikov
Liyo Kao
Xuesi Shao
Debra Newman
Rustam Azimov
Alexander Pushkin
Z. Hong Zhou
Ira Kurtz
author_sort Kevin W. Huynh
title CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
title_short CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
title_full CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
title_fullStr CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
title_full_unstemmed CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1
title_sort cryoem structure of the human slc4a4 sodium-coupled acid-base transporter nbce1
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/8364ae1d1dec4883ada874ff703311fb
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