The lysosomal potassium channel TMEM175 adopts a novel tetrameric architecture

Changkeun Lee, Jiangtao Guo, Weizhong Zeng, Sunghoon Kim, Ji She, Chunlei Cang, Dejian Ren and Youxing Jiang ()
Additional contact information
Changkeun Lee: University of Texas Southwestern Medical Center
Jiangtao Guo: University of Texas Southwestern Medical Center
Weizhong Zeng: University of Texas Southwestern Medical Center
Sunghoon Kim: University of Texas Southwestern Medical Center
Ji She: University of Texas Southwestern Medical Center
Chunlei Cang: University of Pennsylvania
Dejian Ren: University of Pennsylvania
Youxing Jiang: University of Texas Southwestern Medical Center

Nature, 2017, vol. 547, issue 7664, 472-475

Abstract: The lysosomal potassium channel TMEM175 has a tetrameric structure unlike that of the canonical potassium channels, with an hourglass-shaped pore in which isoleucine residues have a key role in channel selectivity.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature23269 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:547:y:2017:i:7664:d:10.1038_nature23269

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature23269

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().