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Literature summary extracted from

  • Beck, E.J.; Yang, Y.; Yaemsiri, S.; Raghuram, V.
    Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating (2008), J. Biol. Chem., 283, 4957-4966.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.6 E1371Q mutation in nucleotide-binding domain 2, prevents ATP hydrolysis without affecting ATP binding and stabilizes the open state of the channel by almost 1000fold Homo sapiens
5.6.1.6 I331C modification rate by methanethiosulfonate ethyl ammonium and (2-sulfonatoethyl) methanethiosulfonate is slower in the open state than in the closed state Homo sapiens
5.6.1.6 K335C modification rate by methanethiosulfonate ethyl ammonium and (2-sulfonatoethyl) methanethiosulfonate is slower in the open state than in the closed state Homo sapiens
5.6.1.6 L333C modification rate by methanethiosulfonate ethyl ammonium and (2-sulfonatoethyl) methanethiosulfonate is slower in the open state than in the closed state Homo sapiens
5.6.1.6 additional information construction of 26 Cys-substituted mutant and analysis of change in cAMP-activated whole cell conductance Homo sapiens
5.6.1.6 R334C modification rate by methanethiosulfonate ethyl ammonium and (2-sulfonatoethyl) methanethiosulfonate is not dependent on open/closed state Homo sapiens
5.6.1.6 T338C modification rate by methanethiosulfonate ethyl ammonium and (2-sulfonatoethyl) methanethiosulfonate is slower in the open state than in the closed state Homo sapiens

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.6 ATP + H2O + closed Cl- channel ATP binding induces a modest conformational change in the sixth transmembrane segment, and this conformational change is coupled to the gating mechanism that regulates ion conduction Homo sapiens ADP + phosphate + open Cl- channel
-
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