Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Csanady, L.; Chan, K.W.; Nairn, A.C.; Gadsby, D.C.
    Functional roles of nonconserved structural segments in CFTRs NH2-terminal nucleotide binding domain (2005), J. Gen. Physiol., 125, 43-55.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.6.1.6 additional information unaltered phosphorylation and ATP dependence of macrosopic current in severed CFTR channels lacking nucleotide-binding domain 1 insertion or extension Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.6 coexpression of CFTR residues 1-414 with residues 433-1480, or residues 1-633 with 668-1480 in Xenopus laevis oocytes, to yield split CFTR channels, that lack most of the insertion or extension, respectively Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.6 additional information deletion of the insertion, but not the extension, of nucleotide-binding domain 1 speeds closing from locked-open bursts, omission of the nucleotide-binding domain 1 insertion or extension causes no major perturbation of the pore architecture Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.1.6 Mg2+
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.6 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.6.1.6 epithelial cell
-
 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
-
 Homo sapiens ADP + phosphate + open Cl- channel
-
 ?

Synonyms

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