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• W1999462422 abstract "Toxins that block voltage-gated potassium (Kv) channels provide a possible template for improved homology models of the Kv pore. In assessing the interactions of Kv channels and their toxins it is important to determine the dynamic flexibility of the toxins. Multiple 10 ns duration molecular dynamics simulations combined with essential dynamics analysis have been used to explore the flexibility of four different Kv channel-blocking toxins. Three toxins (Tc1, AgTx and ChTx) share a common fold. They also share a common pattern of conformational dynamics, as revealed by essential dynamics analysis of the simulation results. This suggests that some aspects of dynamic behaviour are conserved across a single protein fold class. In each of these three toxins, the residue exhibiting minimum flexibility corresponds to a conserved lysine residue that is suggested to interact with the filter domain of the channel. Thus, comparative simulations reveal functionally important conservation of molecular dynamics as well as protein fold across a family of related toxins." @default.
• W1999462422 created "2016-06-24" @default.
• W1999462422 creator A5041718990 @default.
• W1999462422 creator A5077772772 @default.
• W1999462422 date "2002-12-23" @default.
• W1999462422 modified "2023-10-14" @default.
• W1999462422 title "Molecular dynamics simulations of a K⁺ channel blocker: Tc1 toxin from <i>Tityus cambridgei</i>" @default.
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• W1999462422 doi "https://doi.org/10.1016/s0014-5793(02)03849-8" @default.
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