Cargando…
Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2
The chloride ion channel cystic fibrosis transmembrane conductance regulator (CFTR) displays a typical adenosine trisphosphate (ATP)-binding cassette (ABC) protein architecture comprising two transmembrane domains, two intracellular nucleotide-binding domains (NBDs), and a unique intracellular regul...
Autores principales: | Szollosi, Andras, Vergani, Paola, Csanády, László |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2947058/ https://www.ncbi.nlm.nih.gov/pubmed/20876359 http://dx.doi.org/10.1085/jgp.201010434 |
Ejemplares similares
-
Conformational changes in the catalytically inactive nucleotide-binding site of CFTR
por: Csanády, László, et al.
Publicado: (2013) -
Mutant cycles at CFTR’s non-canonical ATP-binding site support little interface separation during gating
por: Szollosi, Andras, et al.
Publicado: (2011) -
Rescue of NBD2 Mutants N1303K and S1235R of CFTR by Small-Molecule Correctors and Transcomplementation
por: Rapino, Daniele, et al.
Publicado: (2015) -
Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel
por: Tsai, Ming-Feng, et al.
Publicado: (2010) -
Nanomechanics combined with HDX reveals allosteric drug binding sites of CFTR NBD1
por: Padányi, Rita, et al.
Publicado: (2022)