ABCC7 p.Asp47Ala
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PMID: 11600681
[PubMed]
Fu J et al: "A cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gating."
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Sentence
Comment
18
Replacing this and two nearby acidic residues with alanines (D47A, E54A, D58A) also reduced channel activity, but had negligible effects on bulk PKA phosphorylation or on the ATP dependence of channel activation.
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ABCC7 p.Asp47Ala 11600681:18:61
status: NEW58 The N-tail triple mutant (D47A, E54A, D58A) was prepared by using the Stratagene site-directed mutagenesis kit.
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ABCC7 p.Asp47Ala 11600681:58:26
status: NEW113 The currents mediated by D58N CFTR were somewhat greater than CFTR channel regulation by the amino tailJ. Physiol. 536.2 those observed for a triple mutant in which three acidic residues were replaced with alanines (D47A, E54A, D58A).
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ABCC7 p.Asp47Ala 11600681:113:218
status: NEW119 D58N CFTR and N-tail triple mutant (D47A, E54A, D58A) exhibit lower macroscopic currents and faster deactivation than wild-type CFTR A, schematic diagram of CFTR topology (left) and helical wheel plot of N-tail region of interest (right) showing locations of the mutations analysed in this study.
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ABCC7 p.Asp47Ala 11600681:119:36
status: NEW228 To further examine the mechanism by which the N-tail modulates ATP-dependent channel gating, we tested the responses of the wild-type and N-tail triple mutant (D47A, E54A, D58A) to ATP and AMP-PNP in single channel studies.
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ABCC7 p.Asp47Ala 11600681:228:160
status: NEW