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Literature summary for 5.6.1.6 extracted from

  • Wang, W.; Linsdell, P.
    Alternating access to the transmembrane domain of the ATP-binding cassette protein cystic fibrosis transmembrane conductance regulator (ABCC7) (2012), J. Biol. Chem., 287, 10156-10165.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression of a human CFTR variant in which all cysteines had been removed by mutagenesis, in baby hamster kidney cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information introduction of Cys residues in a CFTR variant in which all cysteines had been removed by mutagenesis, and patch clamp recording to quantify the rate of access of cysteine-reactive probes. The large [2-sulfonatoethyl]methanethiosulfonate molecule and permeant Au(CN)2- ions, are applied to either side of the membrane to modify cysteines substituted for Leu-102 in the first transmembrane region and Thr-338 in the sixth transmembrane region. Channel opening and closing are altered by mutations in the nucleotide binding domains of the channel. For both [2-sulfonatoethyl]methanethiosulfonate and Au(CN)2-, access to these two cysteines from the cytoplasmic side is faster in open channels, whereas access to these same sites from the extracellular side is faster in closed channels. These results are consistent with alternating access to the transmembrane regions, however with the open state facing inwardly and the closed state facing outwardly Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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