Molecular dynamics simulations of a K+ channel blocker: Tc1 toxin from Tityus cambridgei.

Journal article

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...

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Authors: Grottesi, A; Sansom, MS

• Publication status: Published
• Journal: FEBS letters
• Volume: 535
• Issue: 1-3
• Pages: 29-33
• Publication date: 2003-01-01
• DOI: 10.1016/s0014-5793(02)03849-8
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Charybdotoxin; Models, Molecular; Protein Folding; Animals; Neurotoxins; Protein Conformation; Computer Simulation; Scorpions; Protein Structure, Tertiary; Scorpion Venoms; Conotoxins; Potassium Channel Blockers