Journal
FEBS LETTERS
Volume 535, Issue 1-3, Pages 29-33Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03849-8
Keywords
voltage-gated channel; channel blocker; essential dynamics; molecular simulation
Funding
- Biotechnology and Biological Sciences Research Council [BEP17032, B19456] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [B19456, BEP17032] Funding Source: Medline
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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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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