ABCMdb

ABCC7 p.Lys892Glu

None has been submitted yet.

Publications

PMID: 18449561 [PubMed] Zhou JJ et al: "Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore."

No. Sentence Comment

61 In contrast, K114E, K329E, K892E, and R899E, like wild type, gave almost linear I-V relationships under these conditions. Login to comment
78 The mutations K114E, K329E, K892E, R899E, and R1128E did not affect unitary current amplitude at any voltage (Fig. 4b), consistent with these residues not being involved in Cl- permeation. Login to comment

PMID: 19448737 [PubMed] Zhou JJ et al: "Evidence that extracellular anions interact with a site outside the CFTR chloride channel pore to modify channel properties."

No. Sentence Comment

74 Moreover, reversal of the charge at these sites in ECL4 (in the K892E and R899E mutants) had no effect on unitary Cl-conductance in the presence of high symmetrical Cl- concentrations (Zhou et al. 2008), again consistent with these ECL4 residues not being involved directly in formation of the pore. Login to comment
109 Zhou and Linsdell 391 versing mutations K892E and R899E under different ionic conditions (Zhou et al. 2008). Login to comment

PMID: 25024266 [PubMed] Cui G et al: "Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR."

No. Sentence Comment

117 Fig. S5 illustrates representative single-channel current traces of E116R/ K892E- and R104E/D110R-CFTR and their mean burst durations. Login to comment
224 Tab l e 1 Reversal potentials of WT-CFTR and mutants in ND96 bath solution CFTR n Vrev mV WT 14 &#e032;27.75 &#b1; 0.78 R334A 6 &#e032;12.15 &#b1; 1.64a R117A 6 &#e032;22.51 &#b1; 0.85a E116R 5 &#e032;21.45 &#b1; 1.14a K114D 5 &#e032;24.68 &#b1; 3.22 D110R 5 &#e032;27.64 &#b1; 3.29 R104E 5 &#e032;21.15 &#b1; 1.08a R899C 4 &#e032;25.30 &#b1; 3.94 D891C 6 &#e032;25.81 &#b1; 2.44 K892E 5 &#e032;23.70 &#b1; 3.62 E1124R 5 &#e032;18.32 &#b1; 0.43a E1126R 5 &#e032;20.67 &#b1; 3.16b R117E/E1126R 6 &#e032;23.06 &#b1; 1.37b R104E/E116R 6 &#e032;27.17 &#b1; 1.08 Values are mean &#b1; SEM. Login to comment
301 To test this prediction, we made the single mutation K892E and the double mutation D110R/K892E. Login to comment
302 K892E-CFTR open channels behaved similarly to WT-CFTR, including displaying a stable full open state with single-channel amplitude similar to WT (&#e032;0.77 &#b1; 0.02 pA, n = 5; Fig. 10), outward rectification in the I-V relationship, and WT-like reversal potential (Fig. S4 C and Table 1). Login to comment
304 The double mutant D110R/K892E-CFTR behaved similarly to D110R-CFTR (Fig. 7 A), displaying flickery openings to the s1, s2, and f states with a very brief open burst duration (Fig. 10 A). Login to comment
335 (A) Representative single-channel current traces of K892E-, D110R/K892E-, and D110C/K892C-CFTR recorded with the same experimental conditions as Fig. 2 (left), their all-points amplitude histograms (middle), and their mean burst durations (right). Login to comment
336 *, P < 0.05 indicates a significant difference between D110R- and D110R/K892E-CFTR; #, P < 0.001 for D110C/K892C-CFTR compared with D110R alone. Login to comment
382 E116R/K892E-CFTR exhibited an I-V relationship similar to that of WT-CFTR. Login to comment
383 The burst behavior of E116R/K892E-CFTR was similar to that of E116R-CFTR, suggesting that E116 does not form a salt bridge with K892 when the CFTR channel is in the open state (Fig. S5). Login to comment
437 Top view of the homology model (McCarty laboratory model; Rahman et al., 2013) with salt bridge residues shown as spheres: R117-E1126, red; E116-R104, green; and D110-K892E, magenta. Login to comment