Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions
Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions
About this item
Full title
Author / Creator
Publisher
England: eLife Science Publications, Ltd
Journal title
Language
English
Formats
Publication information
Publisher
England: eLife Science Publications, Ltd
Subjects
More information
Scope and Contents
Contents
CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize occluding two nucleotides at interfacial binding sites; one site hydrolyzes ATP, the other is inactive. The pore opens upon tighte...
Alternative Titles
Full title
Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_f5ece107c12049519b1dda65c7336ac2
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_f5ece107c12049519b1dda65c7336ac2
Other Identifiers
ISSN
2050-084X
E-ISSN
2050-084X
DOI
10.7554/eLife.29013
