ABCC1 p.Asp336Glu
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 15155831
[PubMed]
Haimeur A et al: "Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1)."
No.
Sentence
Comment
5
The overall organic anion transport activity of the same-charge mutant of Asp336 (D336E) also remained very low, as observed for D336R.
X
ABCC1 p.Asp336Glu 15155831:5:82
status: NEW194 For these experiments, GFP-tagged constructs encoding wild-type MRP1 and the mutant MRP1 proteins (D336E, K332D/D336K, K396E, D436K, and R593E) were generated and transfected into HEK 293T cells (Koike et al., 2002).
X
ABCC1 p.Asp336Glu 15155831:194:99
status: NEW208 In a similar way, a like-charge substitution of Glu for Asp at position 336 in the same TM helix of MRP1 resulted in a loss of overall transport activity comparable with that observed with Arg, Lys, or Leu substitutions (Haimeur et al., 2002).
X
ABCC1 p.Asp336Glu 15155831:208:48
status: NEW272 HEK 293T cells were transfected with the wild-type pcDNA3.1(-)-MRP1-GFP and mutant pcDNA3.1(-)-MRP1- D336E-GFP, pcDNA3.1(-)-MRP1-K332D/D336K-GFP, pcDNA3.1(-)- MRP1-K396E-GFP, pcDNA3.1(-)-MRP1-D436K-GFP, and pcDNA3.1(-)- MRP1-R593E-GFP expression vectors as indicated, and cells were viewed 48 h later under the confocal microscope.
X
ABCC1 p.Asp336Glu 15155831:272:101
status: NEW