ABCC1 p.Val1432Gly
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PMID: 19063607
[PubMed]
Qin L et al: "Residues responsible for the asymmetric function of the nucleotide binding domains of multidrug resistance protein 1."
No.
Sentence
Comment
55
Additional mutations (W653Y, V680T, P794A, V1432G, L1437R, and C1439S) were introduced into the dh D793E vector by site-directed mutagenesis using a QuikChange II kit (Stratagene, La Jolla, CA).
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ABCC1 p.Val1432Gly 19063607:55:43
status: NEW56 The forward primers for W653Y, V680T, P794A, V1432G, L1437R, and C1439S were 5'-GCCACATTCACCTATGCCAGGAGC- GAC-3', 5'-GTGGTGGGCCAGACGGGCTGCGGAAAG-3', 5'-TTTA- CCTTCGATGAGGCCCTCTCAGCAGTGGA-3', 5'-AGAAC- CTCAGTGGCGGGCAGCGC-3', and 5'-CAGCGCCAGC- GTGTGAGCCTAGCCCG-3', respectively.
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ABCC1 p.Val1432Gly 19063607:56:45
status: NEW61 To make V1432G, L1437R, and C1439S mutations, a KpnI-ClaI MRP1 DNA fragment was cloned into pBluescript II KS vector, and PCR mutagenesis was performed as described above.
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ABCC1 p.Val1432Gly 19063607:61:8
status: NEW148 The Walker A V680T mutation and the signature C V1432G mutation in NBD2 were without effect, while the double L1437R/C1439S signature C mutation essentially inactivated the D793E protein (Figure 3B).
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ABCC1 p.Val1432Gly 19063607:148:48
status: NEW169 The D793E/V1432G mutation, which did not restore LTC4 transport activity, displayed VO4-independent photolabeling of NBD1 and a decrease in VO4-dependent photolabeling of NBD2 relative to wt MRP1, as observed with the D793E FIGURE 2: Topology of MRP1 showing the positions of conserved asymmetric mutations selected for mutation.
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ABCC1 p.Val1432Gly 19063607:169:10
status: NEW