Cargando…
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...
Autores principales: | Simon, Márton A, Iordanov, Iordan, Szollosi, Andras, Csanády, László |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10569789/ https://www.ncbi.nlm.nih.gov/pubmed/37782012 http://dx.doi.org/10.7554/eLife.90736 |
Ejemplares similares
-
Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates
por: Iordanov, Iordan, et al.
Publicado: (2019) -
Structure of a TRPM2 channel in complex with Ca(2+) explains unique gating regulation
por: Zhang, Zhe, et al.
Publicado: (2018) -
Cryo-EM structures of human ZnT8 in both outward- and inward-facing conformations
por: Xue, Jing, et al.
Publicado: (2020) -
Molecular pathology of the R117H cystic fibrosis mutation is explained by loss of a hydrogen bond
por: Simon, Márton A, et al.
Publicado: (2021) -
Cryo-EM structures of the human glutamine transporter SLC1A5 (ASCT2) in the outward-facing conformation
por: Yu, Xiaodi, et al.
Publicado: (2019)