Cargando…
A flexible GAS belt responds to pore mutations changing the ion selectivity of proton-gated channels
Proton-gated ion channels conduct mainly Na(+) to induce postsynaptic membrane depolarization. Finding the determinants of ion selectivity requires knowledge of the pore structure in the open conformation, but such information is not yet available. Here, the open conformation of the hASIC1a channel...
Autores principales: | Chen, Zhuyuan, Lin, Sheng, Xie, Tianze, Lin, Jin-Ming, Canessa, Cecilia M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8594623/ https://www.ncbi.nlm.nih.gov/pubmed/34766968 http://dx.doi.org/10.1085/jgp.202112978 |
Ejemplares similares
-
A valve-like mechanism controls desensitization of functional mammalian isoforms of acid-sensing ion channels
por: Wu, Yangyu, et al.
Publicado: (2019) -
Structure and analysis of nanobody binding to the human ASIC1a ion channel
por: Wu, Yangyu, et al.
Publicado: (2021) -
Interaction of the Aromatics Tyr-72/Trp-288 in the Interface of the
Extracellular and Transmembrane Domains Is Essential for Proton Gating of
Acid-sensing Ion
Channels
por: Li, Tianbo, et al.
Publicado: (2009) -
Biophysics, pathophysiology, and pharmacology of ion channel gating pores
por: Moreau, Adrien, et al.
Publicado: (2014) -
An arginine residue in the outer segment of hASIC1a TM1 affects both proton affinity and channel desensitization
por: Chen, Zhuyuan, et al.
Publicado: (2021)