Characterization of Kbot21 Reveals Novel Side Chain Interactions of Scorpion Toxins Inhibiting Voltage-Gated Potassium Channels
| Autor: | Najet Srairi-Abid, Mohamed Elayeb, Jan Tytgat, Rym ElFessi-Magouri, Steve Peigneur, Houcemeddine Othman, R. Kharrat |
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| Přispěvatelé: | Obukhov, Alexander G |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Male
Models Molecular PREDICTION Xenopus Molecular Sequence Data Molecular Conformation Scorpion Scorpion Venoms lcsh:Medicine Venom K+-CHANNELS BUTHUS-OCCITANUS-TUNETANUS complex mixtures Mice biology.animal MARTENSI KARSCH Animals Amino Acid Sequence Buthus lcsh:Science Ion channel 3-DIMENSIONAL STRUCTURE Multidisciplinary Science & Technology PURIFICATION biology MAUROTOXIN lcsh:R ANIMAL TOXINS BMBKTX1 Voltage-gated potassium channel biology.organism_classification Molecular biology Potassium channel Molecular Weight Multidisciplinary Sciences Potassium Channels Voltage-Gated Oocytes Biophysics Science & Technology - Other Topics Buthus occitanus lcsh:Q Peptides Sequence Alignment VENOM Research Article Protein Binding |
| Zdroj: | PLoS ONE, Vol 10, Iss 9, p e0137611 (2015) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | Scorpion toxins are important pharmacological tools for probing the physiological roles of ion channels which are involved in many physiological processes and as such have significant therapeutic potential. The discovery of new scorpion toxins with different specificities and affinities is needed to further characterize the physiology of ion channels. In this regard, a new short polypeptide called Kbot21 has been purified to homogeneity from the venom of Buthus occitanus tunetanus scorpion. Kbot21 is structurally related to BmBKTx1 from the venom of the Asian scorpion Buthus martensii Karsch. These two toxins differ by only two residues at position 13 (R /V) and 24 (D/N).Despite their very similar sequences, Kbot21 and BmBKTx1 differ in their electrophysiological activities. Kbot21 targets KV channel subtypes whereas BmBKTx1 is active on both big conductance (BK) and small conductance (SK) Ca2+-activated K+ channel subtypes, but has no effects on Kv channel subtypes. The docking model of Kbot21 with the Kv1.2 channel shows that the D24 and R13 side-chain of Kbot21 are critical for its interaction with KV channels. ispartof: PLOS ONE vol:10 issue:9 ispartof: location:United States status: published |
| Databáze: | OpenAIRE |
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