Cargando…
Engineered high-affinity zinc binding site reveals gating configurations of a human proton channel
The voltage-gated proton channel (H(V)1) is a voltage sensor that also conducts protons. The singular ability of protons to penetrate proteins complicates distinguishing closed and open channels. When we replaced valine with histidine at position 116 in the external vestibule of hH(V)1, current was...
Autores principales: | Cherny, Vladimir V., Musset, Boris, Morgan, Deri, Thomas, Sarah, Smith, Susan M.E., DeCoursey, Thomas E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7537347/ https://www.ncbi.nlm.nih.gov/pubmed/32902579 http://dx.doi.org/10.1085/jgp.202012664 |
Ejemplares similares
-
Aspartate(112) is the Selectivity Filter of the Human Voltage Gated Proton Channel
por: Musset, Boris, et al.
Publicado: (2011) -
Tryptophan 207 is crucial to the unique properties of the human voltage-gated proton channel, hH(V)1
por: Cherny, Vladimir V., et al.
Publicado: (2015) -
The gp91(phox) Component of NADPH Oxidase Is Not a Voltage-gated Proton Channel
por: DeCoursey, Thomas E., et al.
Publicado: (2002) -
Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hH(V)1
por: Morgan, Deri, et al.
Publicado: (2013) -
Histidine(168) is crucial for ΔpH-dependent gating of the human voltage-gated proton channel, hH(V)1
por: Cherny, Vladimir V., et al.
Publicado: (2018)