Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2.

ABSTRACT: 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 regulatory domain. Once phosphorylated in the regulatory domain, CFTR channels can open and close when supplied with cytosolic ATP. Despite the general agreement that formation of a head-to-tail NBD dimer drives the opening of the chloride ion pore, little is known about how ATP binding to individual NBDs promotes subsequent formation of this stable dimer. Structural studies on isolated NBDs suggest that ATP binding induces an intra-domain conformational change termed "induced fit," which is required

SUBMITTER: Szollosi A 

PROVIDER: S-EPMC2947058 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature