Voltage-Sensing Domain of the Third Repeat of Human Skeletal Muscle NaV1.4 Channel As a New Target for Spider Gating Modifier Toxins.
NMR spectroscopy
cell-free protein synthesis
gating modifier toxins
ligand–receptor interaction
sodium channels
Journal
Acta naturae
ISSN: 2075-8251
Titre abrégé: Acta Naturae
Pays: Russia (Federation)
ID NLM: 101525823
Informations de publication
Date de publication:
Historique:
entrez:
7
5
2021
pubmed:
8
5
2021
medline:
8
5
2021
Statut:
ppublish
Résumé
Voltage-gated sodium channels (NaV) have a modular architecture and contain five membrane domains. The central pore domain is responsible for ion conduction and contains a selectivity filter, while the four peripheral voltage-sensing domains (VSD-I/IV) are responsible for activation and rapid inactivation of the channel. "Gating modifier" toxins from arthropod venoms interact with VSDs, influencing the activation and/or inactivation of the channel, and may serve as prototypes of new drugs for the treatment of various channelopathies and pain syndromes. The toxin-binding sites located on VSD-I, II and IV of mammalian NaV channels have been previously described. In this work, using the example of the Hm-3 toxin from the crab spider
Identifiants
pubmed: 33959393
doi: 10.32607/actanaturae.11279
pmc: PMC8084291
doi:
Types de publication
Journal Article
Langues
eng
Pagination
134-139Informations de copyright
Copyright ® 2021 National Research University Higher School of Economics.
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