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• W2012070800 abstract "The aim of our computed study was to examine the possible binding site of primaquine (PQ) using a combined homology protein modeling, automated docking and experimental approach. The target models of wild-type and mutant-types of the voltage-dependent sodium channel in rat skeletal muscle (rNav 1.4) were based on previous work by Tikhonov and Zhorov. Docking was carried out on the P-loop into the structure model of rNav 1.4 channel, in the open state configuration, to identify those amino acidic residues important for primaquine binding. The three-dimensional models of the P-loop segment of wild types and mutant types (W402. W756C, W1239C and W1531A at the outer tryptophan-rich lip, as well as D400C, E755C, K1237C and A1529C of the DEKA motif) helped us to identify residues playing a key role in aminoquinoline binding. In good agreement with experimental results, a 1000-fold inhibition loss was observed, tryptophan 756 is crucial for the reversible blocking effects of PQ. As a result, W756C abolished the blocking effect of primaquine in voltage-clamp assays." @default.
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• W2012070800 date "2012-01-01" @default.
• W2012070800 modified "2023-09-26" @default.
• W2012070800 title "An In-Silico Approach to Primaquine Binding to Trp756 in the External Vestibule of Sodium Channel Nav 1.4" @default.
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• W2012070800 doi "https://doi.org/10.1016/j.bpj.2011.11.1795" @default.
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