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Record Information
Version2.0
Creation Date2009-07-03 22:19:16 UTC
Update Date2014-12-24 20:25:40 UTC
Accession NumberT3D2537
Identification
Common Namealpha-Bungarotoxin
ClassProtein
Descriptionalpha-Bungarotoxin is a peptide toxin produced by the Many-banded krait (Bungarus multicinctus). It is a type of ‘±-neurotoxin, a neurotoxic protein that is known to bind irreversibly and competitively to the acetylcholine receptor found at the neuromuscular junction, causing paralysis, respiratory failure and death in the victim.(4) ‘±-Bungarotoxin (‘±-BTX) is one of the bungarotoxins, components of the venom of the elapid snake Taiwanese banded krait (Bungarus multicinctus). It has also been shown to play an antagonistic role in the binding of the ‘±7 nicotinic acetylcholine receptor in the brain, and as such has numerous applications in neuroscience research.
Compound Type
  • Amide
  • Amine
  • Animal Toxin
  • Natural Compound
  • Organic Compound
  • Protein
  • Snake Venom
Protein StructureT3d2537
Synonyms
Synonym
a-Bungarotoxin
Alpha-Bgt
Alpha-BTX
BGTX
Long neurotoxin 1
Chemical FormulaNot Available
Average Molecular Mass10285.030 g/mol
CAS Registry Number11032-79-4
SequenceNot Available
Chemical Taxonomy
DescriptionNot Available
KingdomOrganic Compounds
Super ClassOrganic Acids
ClassCarboxylic Acids and Derivatives
Sub ClassAmino Acids, Peptides, and Analogues
Direct ParentPeptides
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Actin Filament
  • Cell junction
  • Cell surface
  • Cytoskeleton
  • Cytosol
  • Endoplasmic reticulum
  • Endoplasmic reticulum lumen
  • Extracellular
  • Extracellular matrix
  • Intermediate Filament
  • Membrane Fraction
  • Microsome
  • Microtubule
  • Mitochondrion
  • Nerve Fiber
  • Perinuclear region
  • Plasma Membrane
  • Post Synaptic Density
  • Ribosome
  • Sarcoplasm
  • Sarcoplasmic Reticulum
  • Soluble Fraction
  • Synaptic Vesicle
  • Tubulin
Biofluid LocationsNot Available
Tissue LocationsNot Available
Pathways
NameSMPDB LinkKEGG Link
ApoptosisNot Availablemap04210
Long-term potentiationNot Availablemap04720
EndocytosisNot Availablemap04144
PhenothiazinesNot AvailableNot Available
Insulin secretionNot Availablemap04911
Nicotine addictionNot Availablemap05033
Cell cycleNot Availablemap04110
Antiviral AgentsNot AvailableNot Available
Long-term depressionNot Availablemap04730
Cyclooxygenase InhibitorsNot AvailableNot Available
Cholinergic synapseNot Availablemap04725
Axon guidanceNot Availablemap04360
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateLiquid
AppearanceClear solution.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
Solubility>10 mg/mL
LogPNot Available
Predicted PropertiesNot Available
Spectra
SpectraNot Available
Toxicity Profile
Route of ExposureInjection (sting/bite) (5)
Mechanism of Toxicityalpha-Bungarotoxin binds irreversibly and competitively to muscular and neuronal nicotinic acetylcholine receptors. This produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. (1)
MetabolismFree toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases.
Toxicity ValuesLD50: 0.108 mg/kg (Subcutaneous, Mouse) (6) LD50: 0.113 mg/kg (Intravenous, Mouse) (6) LD50: 0.08 (Intraperitoneal, Mouse) (6)
Lethal DoseNot Available
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/Sourcesalpha-Bungarotoxin is a peptide toxin produced by the Many-banded krait (Bungarus multicinctus). (4)
Minimum Risk LevelNot Available
Health EffectsMany-banded krait bites can cause paralysis, respiratory failure and death. (4)
SymptomsMany-banded krait bites can cause paralysis, respiratory failure and death. (4)
TreatmentAn antivenom exists for Many-banded krait venom. (2)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound ID44264212
ChEMBL IDCHEMBL216458
ChemSpider ID23107257
KEGG IDNot Available
UniProt IDP60615
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDNot Available
Stitch IDalpha-Bungarotoxin
PDB ID1ABT
ACToR IDNot Available
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDST3D2537.pdf
General References
  1. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  2. Wikipedia. Antivenom. Last Updated 1 July 2009. [Link]
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
  4. Wikipedia. alpha-Bungarotoxin. Last Updated 24 June 2009. [Link]
  5. Wikipedia. Snake venom. Last Updated 25 July 2009. [Link]
  6. Thomas S, Griessel E (1999). LD50 Scores for various snakes. [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available

Targets

General Function:
Ion channel activity
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Gene Name:
CHRNA1
Uniprot ID:
P02708
Molecular Weight:
54545.235 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Ligand-gated ion channel activity
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Gene Name:
CHRNB1
Uniprot ID:
P11230
Molecular Weight:
56697.9 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Acetylcholine-activated cation-selective channel activity
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Gene Name:
CHRND
Uniprot ID:
Q07001
Molecular Weight:
58894.55 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Cation transmembrane transporter activity
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Gene Name:
CHRNE
Uniprot ID:
Q04844
Molecular Weight:
54696.54 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Channel activity
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Gene Name:
CHRNG
Uniprot ID:
P07510
Molecular Weight:
57882.8 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Receptor binding
Specific Function:
Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma.
Gene Name:
CHRNA10
Uniprot ID:
Q9GZZ6
Molecular Weight:
49704.295 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Toxic substance binding
Specific Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
Gene Name:
CHRNA7
Uniprot ID:
P36544
Molecular Weight:
56448.925 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]
General Function:
Calcium channel activity
Specific Function:
Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane (PubMed:11752216, PubMed:25282151). The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane (PubMed:11752216, PubMed:25282151). In the ear, this may lead to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma. May also regulate keratinocyte adhesion (PubMed:11021840).
Gene Name:
CHRNA9
Uniprot ID:
Q9UGM1
Molecular Weight:
54806.63 Da
References
  1. Armas LA, Hollis BW, Heaney RP: Vitamin D2 is much less effective than vitamin D3 in humans. J Clin Endocrinol Metab. 2004 Nov;89(11):5387-91. [15531486 ]
  2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 2008;36:D190-D195.
  3. Wikipedia. Arenobufagin. Last Updated 23 January 2009. [Link]