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Literature summary extracted from

  • Hwang, T.C.; Sheppard, D.N.
    Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation (2009), J. Physiol., 587, 2151-2161.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.6 Homo sapiens
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Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
5.6.1.6 phosphoprotein phosphorylation of the unique regulatory domain by the cAMP-dependent protein kinase is a prerequisite for channel opening. CFTR phosphorylation by different kinases might 1. activate, e.g. cGMP-dependent protein kinase II, 2. inhibit, e.g.AMP-activated protein kinase, or 3. have dual effects on channel activity depending on the CFTR construct studied and the consensus phosphorylation site phosphorylated Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.6 ATP + H2O + closed Cl- channel binding mode of ATP in the CFTR nucleotide-binding domain NBD1-NBD2 dimer, organisation of the ATP-binding sites in CFTR involving Walker A and B motifs, and the signature sequence LSGGQ, and conformational changes of the CFTR Cl- channel during channel gating, overview Homo sapiens ADP + phosphate + open Cl- channel
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5.6.1.6 additional information mechanism of action of small molecules that modulate CFTR channel gating Homo sapiens ?
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Subunits

EC Number Subunits Comment Organism
5.6.1.6 More structure modelling, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
5.6.1.6 CFTR
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Homo sapiens