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Literature summary for 5.6.1.6 extracted from

  • Tsai, M.F.; Jih, K.Y.; Shimizu, H.; Li, M.; Hwang, T.C.
    Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels (2010), J. Biol. Chem., 285, 37663-37671.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
transfection of CHO cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
G551D/W401F mutation based on G551D in NBD1 signature motif, which completely abolishes ATP-induced openings of the channel. Additional mutation W401Y become ATP-responsive and are potentiated by N6-2-phenylethyl-ATP Homo sapiens
G551D/W401Y mutation based on G551D in NBD1 signature motif, which completely abolishes ATP-induced openings of the channel. Additional mutation W401Y become ATP-responsive and are potentiated by N6-2-phenylethyl-ATP Homo sapiens
additional information CFTR gating is mainly controlled by ATP binding and hydrolysis in site 2, whereas site 1, which harbors several non-canonical substitutions in ATP-interacting motifs, is considered degenerated. The degenerated site 1 can be rebuilt to complement or support site 2 for CFTR function Homo sapiens
W401F mutation W401Y facilitates channel closure from the lock-open state. W401F appears better than W401Y, which is in turn superior to tryptophan, in stabilizing the lock-open state Homo sapiens
W401Y mutation W401Y facilitates channel closure from the lock-open state. W401F appears better than W401Y, which is in turn superior to tryptophan, in stabilizing the lock-open state Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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