Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.

Abstract excerpt

Thermodynamic mutant cycles provide a formalism for studying energetic coupling between amino acids on the interaction surface in a protein-protein complex. This approach was applied to the Shaker potassium channel and to a high-affinity peptide inhibitor (scorpion toxin) that binds to its pore e...

Topics

• Amino Acid Sequence
• Animals
• Models, Molecular
• Molecular Sequence Data
• Mutation
• Oocytes
• Potassium Channels
• Scorpion Venoms
• Shaker Superfamily of Potassium Channels
• Thermodynamics
• Toxins, Biological
• Xenopus laevis