Cysteine-scanning mutagenesis study of the sixth transmembrane segment of the Na,K-ATPase alpha subunit
Détails
ID Serval
serval:BIB_FA7D4CAD0EA1
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Cysteine-scanning mutagenesis study of the sixth transmembrane segment of the Na,K-ATPase alpha subunit
Périodique
FEBS Letters
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
02/2002
Volume
513
Numéro
2-3
Pages
277-81
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Feb 27
Research Support, Non-U.S. Gov't --- Old month value: Feb 27
Résumé
The accessibility of the residues of the sixth transmembrane segment (TM) of the Bufo marinus Na,K-ATPase alpha subunit was explored by cysteine scanning mutagenesis. Methanethiosulfonate reagents reached only the two most extracellular positions (T803, D804) in the native conformation of the Na,K-pump. Palytoxin induced a conductance in all mutants, including D811C, T814C and D815C which showed no active electrogenic transport. After palytoxin treatment, four additional positions (V805, L808, D811 and M816) became accessible to the sulfhydryl reagent. We conclude that one side of the sixth TM helix forms a wall of the palytoxin-induced channel pore and, probably, of the cation pathway from the extracellular side to one of their binding sites.
Mots-clé
Acrylamides/pharmacology
Animals
Bufonidae/*metabolism
Cysteine/genetics/*metabolism
Indicators and Reagents/pharmacology
Membrane Proteins/drug effects/genetics/*metabolism
Mesylates/pharmacology
Models, Molecular
Mutagenesis, Site-Directed
Na(+)-K(+)-Exchanging ATPase/drug effects/genetics/*metabolism
Transfection
Xenopus laevis
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 13:38
Dernière modification de la notice
20/08/2019 17:25