Publication: Structural basis for ion selectivity in TMEM175 K+ channels
Structural basis for ion selectivity in TMEM175 K+ channels
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Brunner, J. D., Jakob, R. P., Schulze, T., Neldner, Y., Moroni, A., Thiel, G., Maier, T., & Schenck, S. (2020). Structural basis for ion selectivity in TMEM175 K+ channels. ELife, 9, e53683. https://doi.org/10.7554/eLife.53683
Abstract
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Abstract
The TMEM175 family constitutes recently discovered K+ channels that are important for autophagosome turnover and lysosomal pH regulation and are associated with the early onset of Parkinson Disease. TMEM175 channels lack a P-loop selectivity filter, a hallmark of all known K+ channels, raising the question how selectivity is achieved. Here, we report the X-ray structure of a closed bacterial TMEM175 channel in complex with a nanobody fusion-protein disclosing bound K+ ions. Our analysis revealed that a highly conserved layer of threon
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- Brunner, Janine D
- Jakob, Roman P
- Schulze, Tobias
- Neldner, Yvonne
- Moroni, Anna
- Thiel, Gerhard
- Maier, Timm
- Schenck, Stephan
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Brunner, J. D., Jakob, R. P., Schulze, T., Neldner, Y., Moroni, A., Thiel, G., Maier, T., & Schenck, S. (2020). Structural basis for ion selectivity in TMEM175 K+ channels. ELife, 9, e53683. https://doi.org/10.7554/eLife.53683
