Solution Structure of Discrepin, a New K+-Channel Blocking Peptide from the α-KTx15 Subfamily

• Published in: Biochemistry (Easton) Vol. 45; no. 6; pp. 1795 - 1804
• Main Authors: Prochnicka-Chalufour, Ada, Corzo, Gerardo, Satake, Honoo, Martin-Eauclaire, Marie-France, Murgia, Anna Rosa, Prestipino, Gianfranco, D'Suze, Gina, Possani, Lourival D, Delepierre, Muriel
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 14.02.2006
• Subjects: Animals; Binding Sites; Cells, Cultured; Cerebellum - cytology; Chromatography, High Pressure Liquid; Magnetic Resonance Spectroscopy; Models, Molecular; Neurotoxins - chemistry; Potassium Channel Blockers - chemistry; Potassium Channel Blockers - pharmacology; Protein Structure, Secondary; Rats; Rats, Wistar; Scorpion Venoms - chemistry; Scorpion Venoms - isolation & purification; Scorpion Venoms - pharmacology

Discrepin, isolated from the venom of the Venezuelan scorpion Tityus discrepans, blocks preferentially the I A currents of the voltage-dependent K+ channel of rat cerebellum granular cells in an irreversible way. It contains 38 amino acid residues with a pyroglutamic acid as the N-terminal residue [...