ABCC7 p.Lys95Arg
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PMID: 15634668
[PubMed]
Linsdell P et al: "Location of a common inhibitor binding site in the cytoplasmic vestibule of the cystic fibrosis transmembrane conductance regulator chloride channel pore."
No.
Sentence
Comment
69
In a striking parallel with previous findings involving Arg-334 (13, 16), mutagenesis of Lys-95 had a strongly charge-dependent effect on I-V rectification (Fig. 1); the charge-conservative K95R, like wild type CFTR, showed a practically linear I-V relationship, whereas all of the other mutations, and especially the charge-reversing K95E, caused significant outward rectification.
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ABCC7 p.Lys95Arg 15634668:69:190
status: NEW91 These results, using a number of different amino acid substitutions of Lys-95, strongly suggest that side chain charge at this position is important in controlling the apparent affinity of glibenclamide block; the apparent Kd at -100 mV was not affected in the charge-conservative K95R but was significantly increased in charge-neutralizing mutants (K95A, K95C, K95Q) and most strongly increased in the charge-reversing K95E mutant.
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ABCC7 p.Lys95Arg 15634668:91:281
status: NEW
PMID: 17397825
[PubMed]
Zhou JJ et al: "Molecular mechanism of arachidonic acid inhibition of the CFTR chloride channel."
No.
Sentence
Comment
38
Thus, while the charge conservative K95R and R303K mutations were not associated with a significant increase in Kd (PN0.3, two-tailed t-test) all mutations which neutralized or reversed either of these two positive charges were associated with a significant increase in Kd (Fig. 2).
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ABCC7 p.Lys95Arg 17397825:38:36
status: NEW