Literature summary for 5.6.1.6 extracted from

Corradi, V.; Vergani, P.; Tieleman, D.P.
Cystic fibrosis transmembrane conductance regulator (CFTR): closed and open state channel models (2015), J. Biol. Chem., 290, 22891-22906.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Homo sapiens	16020	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P13569	-	-

Synonyms

Synonyms	Comment	Organism
CFTR	-	Homo sapiens
cystic fibrosis transmembrane conductance regulator	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	the enzyme is a member of the ATP-binding cassette (ABC) transporter superfamily, a class of membrane proteins that couple the hydrolysis ofATPwith the transport of molecules across membranes. The enzyme belongs to the ABC-C subfamily (ABC-C7)	Homo sapiens
malfunction	dysfunctional enzyme causes the common lethal genetic disease cystic fibrosis	Homo sapiens
additional information	enzyme structure homology modelling using the crystal structure of four homologous transporters, modelling of open and closed conformations of the enzyme, structural analysis of the transmembrane cavity, detailed overview. Transitions between open and closed states of enzyme CFTR are regulated by ATP binding and hydrolysis on the cytosolic nucleotide binding domains, which are coupled with the transmembrane domains forming the pathway for anion permeation. An important role is played by residue Phe337 as a filter/gating residue	Homo sapiens
physiological function	the enzyme controls Cl- permeation across epithelia as an ABC transporter controling the flow of anions through the apical membrane of epithelia. The ABC protein function as an ion channel rather than as an active transporter	Homo sapiens

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Release 2023.1 (January 2023)