Charged residues at the pore extracellular half of the glycine receptor facilitate channel gating: a potential role played by electrostatic repulsion
Author:
Affiliation:
1. Chern Institute of Mathematics Nankai University Tianjin 300071 China
2. Laboratory for Synaptic Plasticity Shantou University Medical College Shantou Guangdong 515041 China
Funder
National Natural Science Foundation of China
Publisher
Wiley
Subject
Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1113/JP279288
Reference88 articles.
1. Role of Charged Residues in Coupling Ligand Binding and Channel Activation in the Extracellular Domain of the Glycine Receptor
2. Dipoles localized at helix termini of proteins stabilize charges.
3. The Activation Mechanism of 1 Homomeric Glycine Receptors
4. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
5. The impact of human hyperekplexia mutations on glycine receptor structure and function
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