Cryo-EM structure of the polycystin 2-l1 ion channel

We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin...

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Autores principales: Hulse, Raymond E, Li, Zongli, Huang, Rick K, Zhang, Jin, Clapham, David E
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2018
Materias:
Structural Biology and Molecular Biophysics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6056229/
https://www.ncbi.nlm.nih.gov/pubmed/30004384
http://dx.doi.org/10.7554/eLife.36931
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author Hulse, Raymond E
Li, Zongli
Huang, Rick K
Zhang, Jin
Clapham, David E
author_facet Hulse, Raymond E
Li, Zongli
Huang, Rick K
Zhang, Jin
Clapham, David E
author_sort Hulse, Raymond E
collection PubMed
description We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1.
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spelling pubmed-60562292018-07-25 Cryo-EM structure of the polycystin 2-l1 ion channel Hulse, Raymond E Li, Zongli Huang, Rick K Zhang, Jin Clapham, David E eLife Structural Biology and Molecular Biophysics We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1. eLife Sciences Publications, Ltd 2018-07-13 /pmc/articles/PMC6056229/ /pubmed/30004384 http://dx.doi.org/10.7554/eLife.36931 Text en © 2018, Hulse et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Structural Biology and Molecular Biophysics
Hulse, Raymond E
Li, Zongli
Huang, Rick K
Zhang, Jin
Clapham, David E
Cryo-EM structure of the polycystin 2-l1 ion channel
title Cryo-EM structure of the polycystin 2-l1 ion channel
title_full Cryo-EM structure of the polycystin 2-l1 ion channel
title_fullStr Cryo-EM structure of the polycystin 2-l1 ion channel
title_full_unstemmed Cryo-EM structure of the polycystin 2-l1 ion channel
title_short Cryo-EM structure of the polycystin 2-l1 ion channel
title_sort cryo-em structure of the polycystin 2-l1 ion channel
topic Structural Biology and Molecular Biophysics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6056229/
https://www.ncbi.nlm.nih.gov/pubmed/30004384
http://dx.doi.org/10.7554/eLife.36931
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AT huangrickk cryoemstructureofthepolycystin2l1ionchannel
AT zhangjin cryoemstructureofthepolycystin2l1ionchannel
AT claphamdavide cryoemstructureofthepolycystin2l1ionchannel

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