Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein
CFTR, the anion channel mutated in cystic fibrosis patients, is a model ABC protein whose ATP-driven conformational cycle is observable at single-molecule level in patch-clamp recordings. Bursts of CFTR pore openings are coupled to tight dimerization of its two nucleotide-binding domains (NBDs) and...
Main Authors: | Márton A Simon, Iordan Iordanov, Andras Szollosi, László Csanády |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2023-10-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/90736 |
Similar Items
-
Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates
by: Iordan Iordanov, et al.
Published: (2019-04-01) -
ABC transporters and multidrug resistance /
by: Boumendjel, Ahcene, et al.
Published: (2009) -
The ABC transporters of human physiology and disease : genetics and biochemistry of ATP binding cassette transporters /
by: Linton, Kenneth J., et al.
Published: (2011) -
Identification of cisplatin-binding sites on the large cytoplasmic loop of the Na+/K+-ATPase
by: Jaroslava Šeflová, et al.
Published: (2018-01-01) -
Papel de la superfamilia ABC en la resistencia farmacológica
by: Mayasil Morales-Pérez, et al.
Published: (2017-05-01)