Resting state structure of the hyperdepolarization activated two-pore channel 3.
cryoEM
electrophysiology
ion channel
structure
voltage sensors
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
28 01 2020
28 01 2020
Historique:
pubmed:
12
1
2020
medline:
12
5
2020
entrez:
12
1
2020
Statut:
ppublish
Résumé
Voltage-gated ion channels endow membranes with excitability and the means to propagate action potentials that form the basis of all neuronal signaling. We determined the structure of a voltage-gated sodium channel, two-pore channel 3 (TPC3), which generates ultralong action potentials. TPC3 is distinguished by activation only at extreme membrane depolarization (V
Identifiants
pubmed: 31924746
pii: 1915144117
doi: 10.1073/pnas.1915144117
pmc: PMC6995003
doi:
Substances chimiques
Voltage-Gated Sodium Channels
0
Zebrafish Proteins
0
tpcn3 protein, zebrafish
0
Sodium
9NEZ333N27
Banques de données
PDB
['6V1Q']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1988-1993Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM024485
Pays : United States
Organisme : NIAID NIH HHS
ID : T32 AI060537
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM064337
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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