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Literature summary for 5.6.1.6 extracted from

  • Scott-Ward, T.S.; Cai, Z.; Dawson, E.S.; Doherty, A.; Da Paula, A.C.; Davidson, H.; Porteous, D.J.; Wainwright, B.J.; Amaral, M.D.; Sheppard, D.N.; Boyd, A.C.
    Chimeric constructs endow the human CFTR Cl- channel with the gating behavior of murine CFTR (2007), Proc. Natl. Acad. Sci. USA, 104, 16365-16370.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of human-murine CFTR chimeras with sequences from nucleotide-binding domain 1, nucleotide-binding domain 2, or the regulatory domain of human CFTR replaced by the equivalent regions of murine CFTR. The gating behavior of human-murine regulatory domain and human CFTR are indistinguishable, whereas human-murine nucleotide-binding domain 1 and human-murine nucleotide-binding domain 2 have subtle effects on channel gating, prolonging both burst duration and interburst interval. By contrast, human-murine nucleotide-binding domain1-2, containing both nucleotide-binding domains of murine CFTR, reproduces the gating behavior of the subconductance state of murine CFTR, which has dramatically prolonged channel openings Mus musculus
additional information construction of human-murine CFTR chimeras with sequences from nucleotide-binding domain 1, nucleotide-binding domain 2, or the regulatory domain of human CFTR replaced by the equivalent regions of murine CFTR. The gating behavior of human-murine regulatory domain and human CFTR are indistinguishable, whereas human-murine nucleotide-binding domain 1 and human-murine nucleotide-binding domain2 have subtle effects on channel gating, prolonging both burst duration and interburst interval. By contrast, human-murine nucleotide-binding domain1-2, containing both nucleotide-binding domains of murine CFTR, reproduces the gating behavior of the subconductance state of murine CFTR, which has dramatically prolonged channel openings Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 isoform CFTR
-
Mus musculus
-
 isoform CFTR
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel the conformation of nucleotide-binding domain 1 changes before that of nucleotide-binding domain 2 during channel opening. Nucleotide-binding domain dimerization does not proceed by a symmetric tweezer-like motion, but instead in an asymmetric fashion led by nucleotide-binding domain1 Mus musculus
a
ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel the conformation of nucleotide-binding domain1 changes before that of nucleotide-binding domain 2 during channel opening. Nucleotide-binding domain dimerization does not proceed by a symmetric tweezer-like motion, but instead in an asymmetric fashion led by nucleotide-binding domain1 Homo sapiens
a