ABCMdb

PMID: 11087362

Urbatsch IL, Julien M, Carrier I, Rousseau ME, Cayrol R, Gros P
Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein.
Biochemistry. 2000 Nov 21;39(46):14138-49., [PubMed]

Sentences

No. Mutations Sentence Comment

63 ABCB4 p.Glu604Gln A similar strategy was used to create mutants D592N and E604Q. Login to comment 69 ABCB4 p.Glu1125Gln Mutagenic oligos for the D1093N, E1125Q, D1203, and E1249Q mutations were 5'-CTTTGCCATTTA- GAAACAC-3', 5'-GGCAATGTTCTGCGCAATGCTGCAG- TC-3', 5'-TCAGCTCTGAATACAGAAAG-3', and 5'-AAG- GTCAAGCAGCACGGC-3', respectively. Login to comment 137 ABCB4 p.Glu604Gln ABCB4 p.Glu1125Gln Single-point mutations D450N, E482Q, E552Q, D558N, D592N, and E604Q were introduced into the NB1 of Mdr3, and mutations D1093N, E1125Q, E1197Q, D1203N, D1237N, and E1249Q were introduced independently into the NB2. Login to comment 153 ABCB4 p.Glu604Gln ABCB4 p.Glu1125Gln Cells expressing WT Mdr3 or the NB1 mutants D450N, E482Q, D592N, and E604Q (Figure 3A) or their NB2 counterparts D1093N, E1125Q, D1237N, and E1249Q (Figure 3B) were all resistant to FK506. Login to comment 169 ABCB4 p.Glu604Gln ABCB4 p.Glu1125Gln Mating frequencies of mutants D450N (104%), E482Q (127%), D592N (22%), and E604Q (85%) in NB1 (Figure 4) or their counterparts D1093N (72%), E1125Q (101%), D1237N (68%), and E1249Q (118%) in NB2 (Figure 4) were similar to that of the Mdr3 WT control. Login to comment 259 ABCB4 p.Glu604Gln ABCB4 p.Glu1125Gln Single-point mutations D450N, E482Q, D592N, and E604Q were introduced in NB1 and their homologous substitutions D1093N, E1125Q, D1237N, and E1249Q created in NB2, and the mutants were transformed in the yeast S. cereVisiae to assess their biological activity. Login to comment