Nonconventional three-finger toxin BMLCL from krait Bungarus multicinctus venom with high affinity interacts with nicotinic acetylcholine receptors

Nonconventional three-finger toxin BMLCL from krait Bungarus multicinctus venom with high affinity interacts with nicotinic acetylcholine receptors

Nonconventional three-finger toxin BMLCL was isolated from B. multicinctus venom, and its interaction with different subtypes of nicotinic acetylcholine receptor (nAChR) was studied. It was found that BMLCL is able to interact with high efficiency with both α7 and muscle type nAChRs.

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Veröffentlicht in:Doklady. Biochemistry and biophysics 2015-09, Vol.464 (1), p.294-297
Hauptverfasser: Utkin, Yu. N., Kasheverov, I. E., Kudryavtsev, D. S., Andreeva, T. V., Starkov, V. G., Ziganshin, R. H., Kuznetsov, D. V., Anh, Hoang Ngoc, Thao, Nguyen Thi Thanh, Khoa, Nguyen Cuu, Tsetlin, V. I.
Format: Artikel
Sprache:eng
Schlagworte:
Acetylcholine - pharmacology
Amino Acid Sequence
Animals
Aplysia
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Biophysics and Molecular Biology
Bungarotoxins - chemistry
Bungarotoxins - isolation & purification
Bungarotoxins - metabolism
Bungarotoxins - pharmacology
Bungarus
Bungarus multicinctus
Cholinergic Agents - chemistry
Cholinergic Agents - isolation & purification
Cholinergic Agents - metabolism
Cholinergic Agents - pharmacology
Cobra Neurotoxin Proteins - pharmacology
Humans
Life Sciences
Lymnaea
Membrane Potentials - drug effects
Membrane Potentials - physiology
Molecular Sequence Data
Neurons
Nicotine
Oocytes
Rats
Receptors, Nicotinic - metabolism
Reptilian Proteins - chemistry
Reptilian Proteins - isolation & purification
Reptilian Proteins - metabolism
Reptilian Proteins - pharmacology
Sequence Homology, Amino Acid
Toxins
Venom
Xenopus
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Beschreibung
Zusammenfassung:Nonconventional three-finger toxin BMLCL was isolated from B. multicinctus venom, and its interaction with different subtypes of nicotinic acetylcholine receptor (nAChR) was studied. It was found that BMLCL is able to interact with high efficiency with both α7 and muscle type nAChRs.
ISSN:1607-6729
1608-3091
DOI:10.1134/S1607672915050099