ABCC7 p.Glu267Lys

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Publications
PMID: 20089831 [PubMed] Koulov AV et al: "Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis."
No. Sentence Comment
283 Notably, these included C207S, E221A, E267K, D293A, E297A, T298A, and E313A, residues that may contribute to the stability of the Aha1 interaction with Hsp90 (Figures 3 and 4B).
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ABCC7 p.Glu267Lys 20089831:283:38
status: NEW
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PMID: 25190805 [PubMed] Wang W et al: "An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening."
No. Sentence Comment
96 The charge-reversal mutations (E267R and K1060E) at these positions clearly had the most dramatic effects on CFTR activity (the E267K mutation also markedly inhibited CFTR activity; see Fig. 5).
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ABCC7 p.Glu267Lys 25190805:96:128
status: NEW
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138 Fig. 5, A--C confirm this prediction for an E267K/K1060E double mutant.
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ABCC7 p.Glu267Lys 25190805:138:44
status: NEW
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177 Conversely introducing a charge swap double mutation (E267K/K1060E) had no apparent effect on the basal currents and potentiator responses of this truncation construct (Fig. 7, C-E).
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ABCC7 p.Glu267Lys 25190805:177:54
status: NEW
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205 Importantly, normal PKA sensitivity was restored by introducing charge swap mutations across the putative interface (E267K/K1060E; Fig. 9, D-F).
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ABCC7 p.Glu267Lys 25190805:205:117
status: NEW
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241 A, macroscopic current record for a double mutant with charge-reversal substitutions at both positions (E267K/K1060E-CFTR).
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ABCC7 p.Glu267Lys 25190805:241:104
status: NEW
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247 Note that the E267K single mutation strongly inhibited channel activity as did the E267R mutation shown in Fig. 2.
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ABCC7 p.Glu267Lys 25190805:247:14
status: NEW
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325 Symbols are means afe; S.E. Ns are 5, 5, 4, and 5 for WT (black symbols), E267R (red), K1060E (blue), and E267K/K1060E (green), respectively.
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ABCC7 p.Glu267Lys 25190805:325:109
status: NEW
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