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ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator

Muallem, D; Vergani, P; (2009) ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator. Philosophical Transactions of the Royal Society (series B) , 364 (1514) 247 - 255. 10.1098/rstb.2008.0191. Green open access

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Abstract

Proteins belonging to the ATP-binding cassette superfamily couple ATP binding and hydrolysis at conserved nucleotide-binding domains (NBDs) to diverse cellular functions. Most superfamily members are transporters, while cystic fibrosis transmembrane conductance regulator (CFTR), alone, is an ion channel. Despite this functional difference, recent results have suggested that CFTR shares a common molecular mechanism with other members. ATP binds to partial binding sites on the surface of the two NBDs, which then associate to form a NBD dimer, with complete composite catalytic sites now buried at the interface. ATP hydrolysis and gamma-phosphate dissociation, with the loss of molecular contacts linking the two sides of the composite site, trigger dimer dissociation. The conformational signals generated by NBD dimer formation and dissociation are transmitted to the transmembrane domains where, in transporters, they drive the cycle of conformational changes that translocate the substrate across the membrane; in CFTR, they result in opening and closing (gating) of the ion-permeation pathway.

Type: Article
Title: ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator
Open access status: An open access version is available from UCL Discovery
DOI: 10.1098/rstb.2008.0191
Publisher version: http://dx.doi.org/10.1098/rstb.2008.0191
Language: English
Additional information: © 2009 National Academy of Sciences.
Keywords: CFTR, ion channel, ATP-binding cassette transporter, ATP binding and hydrolysis, gating, NUCLEOTIDE-BINDING DOMAINS, ABC TRANSPORTER SUPERFAMILY, CFTR CL-CHANNELS, CRYSTAL-STRUCTURE, SULFOLOBUS-SOLFATARICUS, CHLORIDE CHANNELS, ACTIVE-SITE, SIDE-CHAIN, CASSETTE, CYCLE
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: https://discovery.ucl.ac.uk/id/eprint/173234
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