ABCC1 p.Thr1242Cys
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PMID: 11429411
[PubMed]
Zhang DW et al: "Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17."
No.
Sentence
Comment
134
Thus, Thr1242 was mutated to Ala, Cys, Ser, Leu, Lys, and Asp.
X
ABCC1 p.Thr1242Cys 11429411:134:6
status: NEW248 However, substitution of Thr1242 with either Cys or Ser, which retain hydrogen bonding capability, decreased the ability of the protein to transport E217betaG and to confer drug resistance.
X
ABCC1 p.Thr1242Cys 11429411:248:25
status: NEW
PMID: 17295059
[PubMed]
Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No.
Sentence
Comment
117
Many mutations in TM17, such as Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y, or R1249K, significantly affect MRP1 function [83-86].
X
ABCC1 p.Thr1242Cys 17295059:117:56
status: NEW
PMID: 19949927
[PubMed]
Chang XB et al: "Molecular mechanism of ATP-dependent solute transport by multidrug resistance-associated protein 1."
No.
Sentence
Comment
104
Mutations of C43S in TM1 (112); P343A, K332L and K332D in TM6 (113, 114); W445A and P448A in TM8 (113, 115); T550A, T556A and P557A in TM10 (113, 116); N590A, F594A, P595A, N597A, S604A and S605A in TM11 (113, 117, 118); E1089Q, E1089A, E1089L, E1089N, K1092, S1097 and N1100 in TM14 (119, 120); R1197K in TM16 (121); Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y or R1249K in TM17 (121-124) significantly affect MRP1 function.
X
ABCC1 p.Thr1242Cys 19949927:104:342
status: NEW