ABCMdb

ABCC1 p.Phe1521Tyr

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Publications

PMID: 15459206 [PubMed] Westlake CJ et al: "Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region."

No. Sentence Comment

245 Consistent with a requirement for an aromatic side chain, mutation of Phe1521 to Tyr had no effect on LTC4 transport, whereas substitution with Gly, Gln, or Glu reduced LTC4 transport activity by ϳ60, ϳ70, and ϳ75%, respectively (Table I). Login to comment
256 Related structure COOH-terminal mutation Expression (relative to WT) LTC4 uptake (percentage of WT) Km Vmax -fold % ␮M pmol mg-1 min-1 Helix C3 L1488A 1.2 48 Ϯ 2 I1491A 1.2 59 Ϯ 2 M1492A 1.4 89 Ϯ 3 Sheet C2 V1499A 1.0 94 Ϯ 6 L1500A 1.1 22 Ϯ 1 V1497A/I1498A/V1499A/L1500A 1.0 3.6 Ϯ 0.8 D1501A 1.0 90 Ϯ 5 Sheet C1 G1503A 0.8 100 Ϯ 4 I1505A 0.5 90 Ϯ 10 E1507A 0.8 108 Ϯ 6 G1509A 0.8 113 Ϯ 9 Helix C2 P1511A 1.0 82 Ϯ 6 L1514A/L1515A 1.2 18 Ϯ 2 623 84 L1514V/L1515V 1.0 75 Ϯ 1 L1514I/L1515I 1.0 94 Ϯ 2 Q1516A 1.2 94 Ϯ 3 R1518A 0.8 103 Ϯ 10 G1519A 1.1 100 Ϯ 10 L1520A 1.3 110 Ϯ 3 Helix C1 F1521A 0.8 38 Ϯ 1 F1521Y 1.0 105 Ϯ 2 F1521G 0.9 40 Ϯ 1 F1521Q 1.0 30 Ϯ 1 F1521E 1.0 22 Ϯ 1 Y1522A 1.2 90 Ϯ 5 S1523A 1.1 103 Ϯ 6 M1524A 1.0 130 Ϯ 2 M1524G 1.0 65 Ϯ 3 A1525G 1.0 100 Ϯ 4 M1524G/A1525G 1.0 21 Ϯ 3 733 68 K1526A 2.5 85 Ϯ 2 D1527A/G1529A 3.0 123 Ϯ 4 tation impaired nucleotide binding and trapping at NBD2 to an extent comparable with that resulting from removal of the COOH-terminal 4 amino acids (not shown). Login to comment