Functional dissection of KATP channel structures reveals the importance of a conserved interface.
ABC transporter
ABLOS
Channel gating
Diabetes
KATP
KCO
KNtp
Kir
Kir6
SUR
TMD0
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
01 Dec 2023
01 Dec 2023
Historique:
received:
03
08
2023
revised:
24
10
2023
accepted:
20
11
2023
medline:
16
12
2023
pubmed:
16
12
2023
entrez:
15
12
2023
Statut:
aheadofprint
Résumé
ATP-sensitive potassium channels (KATP) are inhibited by ATP but activated by Mg-ADP, coupling the intracellular ATP/ADP ratio to the potassium conductance of the plasma membrane. Although there has been progress in determining the structure of KATP, the functional significance of the domain-domain interface in the gating properties of KATP channels remains incompletely understood. In this study, we define the structure of KATP as two modules: KATP
Identifiants
pubmed: 38101402
pii: S0969-2126(23)00410-0
doi: 10.1016/j.str.2023.11.008
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.