Key result
A point mutation in the S5-S6 linker region of HERG (S620T) abolished high-affinity block by dofetilide, indicating that important determinants of drug binding are localized to the pore region.
Population
Xenopus oocytes heterologously expressing engineered chimeras between human ether-a-go-go-related gene and…
Comparison
Dofetilide at submicromolar concentrations vs Wild-type HERG and BEAG channels
Design
Preclinical
Authors
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Ser620 critically determines dofetilide-HERG block; extends molecular binding models but leaves clinical translation open.
The serine residue at position 620 in the HERG channel pore region is a critical determinant for high-affinity block by dofetilide, a process closely linked to C-type inactivation.
Ficker et al. (1998) studied HERG K+ channel block. Dofetilide and site-directed mutagenesis vs. Wild-type HERG and BEAG channels was evaluated on High-affinity block by dofetilide and C-type inactivation. A point mutation in the S5-S6 linker region of HERG (S620T) abolished high-affinity block by dofetilide, indicating that important determinants of drug binding are localized to the pore region.
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