Article
Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3.
Biochemistry - 8 Oct 2002
Lanigan Mark D, Kalman Katalin, Lefievre Yann, Pennington Michael W, Chandy K George, Norton Raymond S
Abstract excerpt
The voltage-gated potassium channel in T lymphocytes, Kv1.3, an important target for immunosuppressants, is blocked by picomolar concentrations of the polypeptide ShK toxin and its analogue ShK-Dap22. ShK-Dap22 shows increased selectivity for Kv1.3, and our goal was to determine the molecular basis for this selectivity by probing the interactions of ShK and ShK-Dap22 with the pore and vestibule of Kv1.3. The free...
Topics
- Binding Sites
- Cnidarian Venoms
- Kv1.3 Potassium Channel
- Ligands
- Lysine
- Models, Molecular
- Mutation
- Potassium Channels
- Potassium Channels, Voltage-Gated
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- Thermodynamics