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- W2042040973 abstract "The carboxyl terminus of S3 segment (S3C) in voltage-gated potassium channels was proposed to bear the binding site for gating modifier toxins like Hanatoxin and a helical secondary structural arrangement was suggested. Due to the lack of complete structure in high resolution for such a channel molecule, no further direct experimental data to elucidate the mechanism for their binding conformations could thus far be derived. In order to examine the putative three-dimensional structure of S3C and to illustrate the residues required for Hanatoxin binding, molecular simulation and docking were performed, based on the solution structure of Hanatoxin and the structural information from lysine-scanning results for S3C fragment. From our results, it is indicated that both hydrophobic and electrostatic interactions are utilized to stabilize the toxin binding. Detailed docking residues and appropriate orientation for binding regarding hydrophobic/-philic environments are also described. Compared with the functional data proposed by previous studies, the helical structural arrangement for the C-terminus of S3 segment in voltage-gated potassium channels can therefore be further emphasized. Copyright © 2002 John Wiley & Sons, Ltd." @default.
- W2042040973 created "2016-06-24" @default.
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- W2042040973 date "2002-01-01" @default.
- W2042040973 modified "2023-09-29" @default.
- W2042040973 title "Molecular determinants of the hanatoxin binding in voltage-gated K+-channel drk1" @default.
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- W2042040973 doi "https://doi.org/10.1002/jmr.571" @default.
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