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Literature summary for 5.6.1.6 extracted from

  • Mense, M.; Vergani, P.; White, D.M.; Altberg, G.; Nairn, A.C.; Gadsby, D.C.
    In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer (2006), EMBO J., 25, 4728-4739.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.6

Activating Compound

Activating Compound Comment Organism Structure
ATP half-maximal activation by 0.05 mM Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in Xenopus laevis Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information mutation C590V/592V plus mutation of the remaining 16 Cys residues to Ser, or mutation C590L/592L plus mutation of the remaining 16 Cys residues to Ser results in a mutant protein with about 30% of wild-type activity. This Cys-free mutant allows for the sequential introduction of target Cys residues for cross-linking studies. Introduction of S1248C, S549C, S605C, A1374C, A462C, S1347C into the Cys-free mutant and analysis of crosslinks demonstrates that nucleotide-binding domains 1 and 2 interact in a head-to-tail configuration. Protein phosphorylation by protein kinase A promotes formation of the nucleotide-binding domain heterodimer Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P13569 isoform CFTR
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein nucleotide-binding domains 1 and 2 interact in head-to-tail configuration. Protein phosphorylation by protein kinase A promotes formation of the nucleotide-binding domain heterodimer Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CFTR protein channel requires phosphorylation by PKA before they can be opened by ATP, close upon ATP removal, and are activated half-maximally by 0.05 mM ATP Homo sapiens ?
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Subunits

Subunits Comment Organism
More nucleotide-binding domains 1 and 2 interact in head-to-tail configuration. Protein phosphorylation by protein kinase A promotes formation of the nucleotide-binding domain heterodimer Homo sapiens