ABCMdb

ABCC7 p.Lys95Glu

None has been submitted yet.

Publications

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. Login to comment
91 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. Login to comment

PMID: 17178710 [PubMed] Wang W et al: "Curcumin opens cystic fibrosis transmembrane conductance regulator channels by a novel mechanism that requires neither ATP binding nor dimerization of the nucleotide-binding domains."

No. Sentence Comment

143 D, curcumin also stimulates K95E/⌬1198-CFTR currents, which showstrongoutwardrectification.Inset,I-Vcurvesforcontrol(curve1),afteraddingcurcumin(curve2),afterre-addingcurcuminwithnoATP(curve3),andafter curcuminwashout(curve4).E,curcumintitrationfor⌬1198-CFTRchannelsintheabsenceofbathATP.Inset,meantitrationdatafittoasingleMichaelis-Menten function(EC50 ϭ20.8Ϯ5.4␮M,nϭ4).F,curcuminalsoactivatesW1282X-CFTRchannels.Alloftherecordsarerepresentativeofatleastfourexperimentsexcept D (n ϭ 2). Login to comment
144 ATP-independent CFTR Channel Gating Because the ⌬1198-CFTR construct is new to the CFTR field, we validated that the currents that are mediated by this construct are authentic CFTR currents in two ways: (i) by performing unitary currents recordings, which confirmed that this NBD2 deletion construct exhibits the appropriate single channel conductance (6-8 pS) and linear I-V behavior expected for CFTR channels (Fig. 3) (5, 6) and (ii) by introducing a point mutation (K95E) in this deletion construct that had been shown by Linsdell (30) to induce strong outward rectification of the currents mediated by the full-length channel. Login to comment
145 Fig. 2D shows that the currents mediated by K95E/⌬1198-CFTR exhibit strong outward rectification, as expected, and that these rectifying currents are robustly activated by curcumin. Login to comment

PMID: 9379167 [PubMed] Tabcharani JA et al: "Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels."

No. Sentence Comment

264 Arg347 May Contribute to a Weak Field Strength Site for Iodide High macroscopic PI/PCl ratios have been reported previously for CFTR channels in which positively charged residues in the membrane spanning regions were mutated to negatively charged residues (K95E, 1.43; K335E, 1.37; R347E, 0.9; R1030E, 0.81; Anderson et al., 1991). Login to comment
289 Arg347 May Contribute to a Weak Field Strength Site for Iodide High macroscopic PI/PCl ratios have been reported previously for CFTR channels in which positively charged residues in the membrane spanning regions were mutated to negatively charged residues (K95E, 1.43; K335E, 1.37; R347E, 0.9; R1030E, 0.81; Anderson et al., 1991). Login to comment