Movatterモバイル変換


[0]ホーム

URL:


Jump to content
WikipediaThe Free Encyclopedia
Search

β-Bungarotoxin

From Wikipedia, the free encyclopedia
Chemical compound
β-Bungarotoxin
Schematic diagram of the three-dimensionalstructure of β2-bungarotoxin (PDB:1bun​)
Identifiers
OrganismBungarus multicinctus
SymbolN/A
CAS number12778-32-4
β1:65862-89-7
β2:82446-04-6

β-Bungarotoxin is a form ofbungarotoxin that is fairly common inKrait (Bungarus multicinctus)venoms. It is the prototypic class of snake β-neurotoxins. There are at least five isoforms, coded β1 to β5, assembled from different combinations of A and Bchains.[1]

The toxin is a heterodimer of two chains. The A chain confersphospholipase A2 (PLP A2) activity, and the B chain, likedendrotoxins, have aKunitz domain. There are many isoforms of these chains: examples of A chains include A1 (P00617), A3 (P00619), and A4 (P17934), and examples of B chains include B2 (P00989) and B3 (Q75S50). The B chain plays a functional role in inducing apoptosis.[2]

The target of this neurotoxin is at thepresynaptic terminal, where it blocks release ofacetylcholine. It seems to do so by blocking the phosphorylation ofMARCKS.[3] It is thought that the dendrotoxin-like B chain acts first by inhibition of ion channels, causing cessation of twitches followed by a prolonged facilitatory phase. The A chain (bearing phospholipase activity) then induces a blocking phase by destruction of phospholipids.[4]

Binding sites

[edit]

Neurobiological research from the late 1980s has found that beta-bungarotoxin selectively binds to (125)I-DTX-I receptor.

See also

[edit]

References

[edit]
  1. ^Kondo, K; Toda, H; Narita, K; Lee, CY (May 1982). "Amino acid sequences of three beta-bungarotoxins (beta 3-, beta 4-, and beta 5- bungarotoxins) from Bungarus multicinctus venom. Amino acid substitutions in the A chains".Journal of Biochemistry.91 (5):1531–48.doi:10.1093/oxfordjournals.jbchem.a133844.PMID 7096305.
  2. ^Cheng YC, Wang JJ, Chang LS (February 2008). "B chain is a functional subunit of beta-bungarotoxin for inducing apoptotic death of human neuroblastoma SK-N-SH cells".Toxicon.51 (2):304–15.Bibcode:2008Txcn...51..304C.doi:10.1016/j.toxicon.2007.10.006.PMID 18037462.
  3. ^Ueno, E; Rosenberg, P (1996). "Mechanism of action of beta-bungarotoxin, a presynaptically acting phospholipase A2 neurotoxin: its effect on protein phosphorylation in rat brain synaptosomes".Toxicon.34 (11–12):1219–27.doi:10.1016/S0041-0101(96)00113-4.PMID 9027977.
  4. ^Rowan, EG (January 2001). "What does beta-bungarotoxin do at the neuromuscular junction?".Toxicon.39 (1):107–18.Bibcode:2001Txcn...39..107R.doi:10.1016/S0041-0101(00)00159-8.PMID 10936627.
Bacterial
toxins
Exotoxin
Gram
positive
Bacilli
Clostridium:
Other:
Cocci
Staphylococcus
Actinomycetota
Gram
negative
Mechanisms
Endotoxin
Virulence
factor
Mycotoxins
Plant toxins
Invertebrate
toxins
Scorpion:
Spider:
Mollusca:
Vertebrate
toxins
Fish:
Amphibian:
Reptile/
Snake venom:
  • note: some toxins are produced by lower species and pass through intermediate species
Enzyme
(modulators)
ChATTooltip Choline acetyltransferase
AChETooltip Acetylcholinesterase
BChETooltip Butyrylcholinesterase
Transporter
(modulators)
CHTTooltip Choline transporter
VAChTTooltip Vesicular acetylcholine transporter
Release
(modulators)
Inhibitors
Enhancers


Stub icon

Thisdrug article relating to thenervous system is astub. You can help Wikipedia byexpanding it.

Retrieved from "https://en.wikipedia.org/w/index.php?title=Β-Bungarotoxin&oldid=1264683190"
Categories:
Hidden categories:

[8]ページ先頭

©2009-2025 Movatter.jp