Slotoxin, aKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between a and a+ß (ß1 or ß4) complexes
Por:
Garcia-Valdes J., Zamudio F.Z., Toro L., Possan L.D.
Publicada:
1 ene 2001
Resumen:
A novel peptide from Centruroides noxius Hoffmann scorpion venom was isolated and sequenced. The 37 amino acid peptide belongs to the charybdotoxin sub-family (?KTx1) and was numbered member 11. ?KTx1.11 has 75% sequence identity with iberiotoxin and 54% with charybdotoxin. ?KTx1.11 revealed specificity for mammalian MaxiK channels (hSlo), thus, was named slotoxin. Slotoxin blocks the MaxiK pore-forming ? subunit reversibly (Kd = 1.5 nM). Slotoxin association with ?+? (?1 or ?4) channels was ? 10 times slower than iberiotoxin and charybdotoxin, leading to a lack of effect on ?+?4 when tested at 100 nM for 5 min. Thus, slotoxin is a better tool to distinguish MaxiK ?+? complexes. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Filiaciones:
Garcia-Valdes J.:
Department of Molecular Recognition and Structural Biology, Inst. of Biotech., Natl. Autonomous University of Mexico, Avenida Universidad 2001, Cuernavaca 62210, Mexico
Zamudio F.Z.:
Department of Molecular Recognition and Structural Biology, Inst. of Biotech., Natl. Autonomous University of Mexico, Avenida Universidad 2001, Cuernavaca 62210, Mexico
Toro L.:
Departments of Anesthesiology and Molecular and Medical Pharmacology, Brain Research Institute, University of California, Los Angeles, CA 90095-7115, United States
Possan L.D.:
Department of Molecular Recognition and Structural Biology, Inst. of Biotech., Natl. Autonomous University of Mexico, Avenida Universidad 2001, Cuernavaca 62210, Mexico
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