ABCB1 p.Ile306Glu
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PMID: 15379547
[PubMed]
Loo TW et al: "The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium."
No.
Sentence
Comment
48
Histidine-tagged wild-type P-gp and mutants I306E and I306R were constructed as described previously (35, 36).
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ABCB1 p.Ile306Glu 15379547:48:44
status: NEW113 Therefore, an alternative approach to introduce a charged group at position 306 would be to mutate Ile306 to glutamic acid or arginine.
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ABCB1 p.Ile306Glu 15379547:113:99
status: NEW123 Histidine-tagged wild-type and mutants I306E and I306R P-gps were expressed in HEK 293 cells, isolated by nickel-chelate chromatography and mixed with lipid, and verapamil-stimulated ATPase activity was determined.
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ABCB1 p.Ile306Glu 15379547:123:39
status: NEW124 Figure 4 shows that mutation of Ile306 to glutamic acid or arginine significantly affected the apparent affinity for verapamil.
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ABCB1 p.Ile306Glu 15379547:124:32
status: NEW125 The wild-type P-gp and mutants I306R and I306E showed maximal stimulation of 16.1-, >10.8-, and 7-fold and S50 (concentration required for 50% stimulation) of 44, >2200, and 305 µM, respectively.
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ABCB1 p.Ile306Glu 15379547:125:41
status: NEW139 HEK 293 cells were transfected with wild-type P-gp or with P-gp mutants I306E or I306R (in wild-type background) cDNAs. After 24 h, the medium was replaced with fresh medium.
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ABCB1 p.Ile306Glu 15379547:139:72
status: NEW143 FIGURE 4: Verapamil-stimulated ATPase activity of wild-type and mutant I306R and I306E P-gps.
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ABCB1 p.Ile306Glu 15379547:143:81
status: NEW144 Histidine-tagged wild-type, mutant I306R or mutant I306E P-gps were expressed in HEK 293 cells and isolated by nickel-chelate chromatography.
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ABCB1 p.Ile306Glu 15379547:144:51
status: NEW