Analysis of the structural and molecular basis of voltage-sensitive sodium channel inhibition by the spider toxin huwentoxin-IV (μ-TRTX-Hh2a)

Abstract

Background: The molecular basis for sodium channel inhibition by spider venom peptides is poorly understood. Results: Key toxin residues and structural features important for activity of huwentoxin-IV are identified. Conclusion: Toxin activity involves a hydrophobic protrusion surrounded by a ring of basic residues. Significance: New structure-function information may provide a foundation for the design of peptides with therapeutic potential. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.