1v7f
Solution structure of phrixotoxin 1
Structural highlights
FunctionTXP1_PARSR Potently blocks A-type potassium currents. Specifically blocks Kv4.2/KCND2 and Kv4.3/KCND3 channels by altering the gating properties of these channels.[1] Publication Abstract from PubMedAnimal toxins block voltage-dependent potassium channels (Kv) either by occluding the conduction pore (pore blockers) or by modifying the channel gating properties (gating modifiers). Gating modifiers of Kv channels bind to four equivalent extracellular sites near the S3 and S4 segments, close to the voltage sensor. Phrixotoxins are gating modifiers that bind preferentially to the closed state of the channel and fold into the Inhibitory Cystine Knot structural motif. We have solved the solution structure of Phrixotoxin 1, a gating modifier of Kv4 potassium channels. Analysis of the molecular surface and the electrostatic anisotropy of Phrixotoxin 1 and of other toxins acting on voltage-dependent potassium channels allowed us to propose a toxin interacting surface that encompasses both the surface from which the dipole moment emerges and a neighboring hydrophobic surface rich in aromatic residues. Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus.,Chagot B, Escoubas P, Villegas E, Bernard C, Ferrat G, Corzo G, Lazdunski M, Darbon H Protein Sci. 2004 May;13(5):1197-208. PMID:15096626[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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