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Br J Pharmacol
2000 Dec 01;1318:1503-6. doi: 10.1038/sj.bjp.0703734.
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Molecular impact of MinK on the enantiospecific block of I(Ks) by chromanols.
Lerche C
,
Seebohm G
,
Wagner CI
,
Scherer CR
,
Dehmelt L
,
Abitbol I
,
Gerlach U
,
Brendel J
,
Attali B
,
Busch AE
.
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Slowly activating I:(Ks) (KCNQ1/MinK) channels were expressed in Xenopous: oocytes and their sensitivity to chromanols was compared to homomeric KCNQ1 channels. To elucidate the contribution of the ss-subunit MinK on chromanol block, a formerly described chromanol HMR 1556 and its enantiomer S5557 were tested for enantio-specificity in blocking I:(Ks) and KCNQ1 as shown for the single enantiomers of chromanol 293B. Both enantiomers blocked homomeric KCNQ1 channels to a lesser extent than heteromeric I:(Ks) channels. Furthermore, we expressed both WT and mutant MinK subunits to examine the involvement of particular MinK protein regions in channel block by chromanols. Through a broad variety of MinK deletion and point mutants, we could not identify amino acids or regions where sensitivity was abolished or strikingly diminished (>2.5 fold). This could indicate that MinK does not directly take part in chromanol binding but acts allosterically to facilitate drug binding to the principal subunit KCNQ1.
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