ABCC1 p.Asn1100Ser
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PMID: 12954620
[PubMed]
Zhang DW et al: "Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding state."
No.
Sentence
Comment
51
They are as follows: T1082A (5Ј-C TCC AAG GAG CTC GAC GCA GTG GAC TCC-3Ј), D1084N (5Ј-CTG GAC ACA GTG AAT TCC ATG ATC CCG-3Ј), D1084A (5Ј-CTG GAC ACA GTG AAA TCG ATG ATC CCG-3Ј), D1084E (5Ј-CTG GAC ACA GTG GAC TCG ATG ATC CCG-3Ј), D1084V (5Ј-CTG GAC ACA GTG GTA TCG ATG ATC CCG-3Ј), S1085A (5Ј-CTG GAC ACA GTC GAC GCC ATG ATC CCG G-3Ј), K1092M (5Ј-C CCG GAG GTC ATC ATG ATG TTC ATG GGC-3Ј), K1092A (5Ј-C CCG GAG GTC ATC GCG ATG TTC ATG GGC-3Ј), K1092E (5Ј-C CCG GAG GTC ATC GAG ATG TTC ATG GGC-3Ј), K1092R (5Ј-C CCG GAG GTC ATC AGG ATG TTC ATG GGC-3Ј), S1097A (5Ј-G ATG TTC ATG GGC GCC CTG TTC AAC-3Ј), N1100A (5Ј-TTC ATG GGC TCG CTC TTC GCC GTC ATT GGT G-3Ј), N1100S (5Ј-TTC ATG GGC TCG CTC TTC AGT GTC ATT GGT G-3Ј).
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ABCC1 p.Asn1100Ser 12954620:51:805
status: NEW218 Effects of Mutations D1084A, D1084E, D1084V, D1084R, K1092A, K1092E, K1092R, and N1100S on Transport of [3 H]LTC4 and [3 H]E217betaG by Wild Type MRP1-Because mutation D1084N dramatically affected all of the MRP1 functions tested, we also mutated Asp1084 to Ala, Glu, Arg, and Val.
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ABCC1 p.Asn1100Ser 12954620:218:81
status: NEW235 Consequently, we also mutated Asn1100 to Ser, as it is in the rodent proteins.
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ABCC1 p.Asn1100Ser 12954620:235:30
status: NEW240 Mutation N1100S, like N1100A, decreased only E217betaG transport.
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ABCC1 p.Asn1100Ser 12954620:240:9
status: NEW247 Mutation N1100S had no effect on the drug profile of MRP1.
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ABCC1 p.Asn1100Ser 12954620:247:9
status: NEW278 On the other hand, mutations S1097A, N1100A, and N1100S reduced E217betaG but not LTC4 or GSH transport activity.
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ABCC1 p.Asn1100Ser 12954620:278:49
status: NEW