ABCC8 p.Met1289Leu
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PMID: 15561900
[PubMed]
Hambrock A et al: "Effect of two amino acids in TM17 of Sulfonylurea receptor SUR1 on the binding of ATP-sensitive K+ channel modulators."
No.
Sentence
Comment
96
As we intended to compare binding properties of SUR1 with the mutants SUR1(T1285L, M1289L) and SUR1(M1289L), [3 H]glibenclamide was chosen as the radioligand due to its high affinity to SUR1.
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ABCC8 p.Met1289Leu 15561900:96:83
status: NEWX
ABCC8 p.Met1289Leu 15561900:96:100
status: NEW100 Displacing [3 H]glibenclamide by increasing concentrations of unlabeled glibenclamide (Fig. 2A) resulted in similar monophasic inhibition curves for SUR1, SUR1 (M1289L), and SUR1(T1285L, M1289L) with KD values of thioformamide: aprikalim [F]; and benzothiadiazine: diazoxide [G].
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ABCC8 p.Met1289Leu 15561900:100:161
status: NEWX
ABCC8 p.Met1289Leu 15561900:100:187
status: NEW111 Glibenclamide binding was not significantly changed by the mutations [pKi SUR1 (M1289L) vs. SUR1: P ϭ 0.0868; pKi SUR1(T1285L, M1289L) vs. SUR1: P ϭ 0.0825].
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ABCC8 p.Met1289Leu 15561900:111:80
status: NEWX
ABCC8 p.Met1289Leu 15561900:111:133
status: NEW112 In the following experiments, binding of openers representative of different chemical classes was systematically compared between SUR1 and SUR1(T1285L, M1289L); for P1075, levcromakalim, and diazoxide, the mutant SUR1 (M1289L) was also investigated.
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ABCC8 p.Met1289Leu 15561900:112:152
status: NEWX
ABCC8 p.Met1289Leu 15561900:112:219
status: NEW118 Binding of P1075 to SUR1(T1285L, M1289T) did not differ much from binding to SUR1(M1289L) (Table 1).
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ABCC8 p.Met1289Leu 15561900:118:82
status: NEW