期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1865, 期 5, 页码 465-472出版社
ELSEVIER
DOI: 10.1016/j.bbapap.2017.02.001
关键词
Scorpion toxins; Voltage-gated potassium channels; Pore blockers; Cysteine-stabilized alpha/beta fold (CS alpha/beta); KTx
资金
- Russian Science Foundation [14-14-00239]
- F.W.O.-Vlaanderen [G.0433.12, GOE3414N]
- Inter-University Attraction Poles Program, Belgian State, Belgian Science Policy [IUAP 7/10]
- scholarship of the President of the Russian Federation for young scientists and postgraduate students [CII-2634.2016.4]
- St. Petersburg Polytechnic University
- Russian Academic Excellence [5-100]
- KU Leuven [OT/12/081]
- Russian Science Foundation [14-14-00239] Funding Source: Russian Science Foundation
We report isolation, sequencing, and electrophysiological characterization of OSK3 (alpha-KTx 8.8 in Kalium and Uniprot databases), a potassium channel blocker from the scorpion Orthochirus scrobiculosus venom. Using the voltage clamp technique, OSK3 was tested on a wide panel of 11 voltage-gated potassium channels expressed in Xenopus oocytes, and was found to potently inhibit Kv1.2 and Kv1.3 with IC50 values of similar to 331 nM and similar to 503 nM, respectively. OdK1 produced by the scorpion Odontobuthus doriae differs by just two C-terminal residues from OSK3, but shows marked preference to Kv1.2. Based on the charybdotoxin-potassium channel complex crystal structure, a model was built to explain the role of the variable residues in OdK1 and OSK3 selectivity. (C) 2017 Elsevier B.V. All rights reserved.
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