ABCMdb

ABCC3 p.Trp1242Pro

None has been submitted yet.

Publications

PMID: 12388190 [PubMed] Oleschuk CJ et al: "Substitution of Trp1242 of TM17 alters substrate specificity of human multidrug resistance protein 3."

No. Sentence Comment

70 G281CONSERVED ACA TTC GCT TTA AAC TTC ATG ATA CGA ATG ATG TCA G-3Ј), W1242Y (5Ј-G CAG GTG ACA TTC GCT TTA AAC TAC ATG ATA CGA ATG ATG TCA G-3Ј), and W1242P (5Ј-G CAG GTG ACA TTC GCT TTA AAC CCG ATG ATA CGA ATG ATG TCA G-3Ј). Login to comment
104 Trp1242 was also replaced with a ␣-helix-disrupting residue (Pro; W1242P-MRP3). Login to comment
107 In contrast, the W1242P-MRP3 mutant was expressed at significantly lower levels, suggesting that this mutation affects the biogenesis or stability of the protein. Login to comment
108 Mean expression levels of the mutant MRP3 proteins relative to wild-type MRP3 were as follows: W1242A, 1.1 Ϯ 0.3; W1242C, 1.0 Ϯ 0.2; W1242Y, 1.0 Ϯ 0.1; W1242F, 1.0 Ϯ 0.3; and W1242P, 0.6 Ϯ 0.2 (4-6 independent transfections). Login to comment
110 Time courses of ATP-dependent [3 H]E217betaG uptake were determined for the W1242A-, W1242C-, W1242F-, W1242Y-, and W1242P-MRP3 mutants by using inside-out membrane vesicles prepared from transfected HEK293T cells (Fig. 3A). Login to comment
112 In contrast, transport by W1242P-MRP3 was almost undetectable. Login to comment
122 [3 H]LTC4 uptake by the W1242P-MRP3 mutant was undetectable (not shown). Login to comment
123 Because of the consistently lower levels of W1242P-MRP3 expression and because this mutant did not transport either E217betaG or LTC4, it was not characterized further. Login to comment
130 A: time course of ATP-dependent [3 H]E217betaG uptake in membrane vesicles prepared from HEK293T cells transfected with empty vector (ᮀ), wild-type MRP3 (s), and mutant [W1242A (), W1242C (}), W1242F (F), W1242Y (Œ), and W1242P (ƒ)] cDNA expression vectors. Login to comment
135 Top: MRP3 expression in membrane vesicles prepared from human embryonic kidney (HEK) 293T cells transfected with empty vector [pcDNA3.1(ϩ)], wild-type (WT-MRP3), and mutant (W1242A, W1242C, W1242F, W1242Y, and W1242P) MRP3 cDNAs was determined by immunoblotting with MAb M3II-9, and relative levels of expression were estimated by densitometry. Login to comment
199 Transport activities of variously substituted MRP3-Trp1242 mutants Substrate Transport Activity W1242A W1242C W1242F W1242Y W1242P E217betaG 1 1 1 11 222 LTC4 2 22 2 2 222 MTX 222 222 222 222 n.d. Login to comment
217 The loss of H-bonding and aromatic stacking interactions alone cannot fully account for the inactivity of the W1242P-MRP3 mutant, because the Ala, Cys, Phe, and Tyr mutants all retained some transport activity. Login to comment