About: Scorpion toxin     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : yago:Unit108189659, within Data Space : dbpedia.org associated with source document(s)
QRcode icon
http://dbpedia.org/describe/?url=http%3A%2F%2Fdbpedia.org%2Fresource%2FScorpion_toxin

Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal- or insect-specific and acts by binding with varying degrees of specificity to members of the Voltage-gated ion channel superfamily; specifically, voltage-gated sodium channels, voltage-gated potassium channels, and Transient Receptor Potential (TRP) channels. The result of this action is to activate or inhibit the action of these channels in the nervous and cardiac organ systems. For instance, α-scorpion toxins MeuNaTxα-12 and MeuNaTxα-13 from Mesobuthus eupeus are neurotoxins that target voltage-gated Na+ channels (Navs), inhibiting fast inactivation. In vivo assays of MeuNaTxα-12 and MeuNaTxα-13 effects on mammalian and insect Navs show differential potency. These recombinants (MeuNaTxα-12 and

AttributesValues
rdf:type
rdfs:label
  • Skorpiontoxin (de)
  • Scorpion toxin (en)
rdfs:comment
  • Ein Skorpiontoxin ist ein Toxin, das von Skorpionen gebildet wird. (de)
  • Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal- or insect-specific and acts by binding with varying degrees of specificity to members of the Voltage-gated ion channel superfamily; specifically, voltage-gated sodium channels, voltage-gated potassium channels, and Transient Receptor Potential (TRP) channels. The result of this action is to activate or inhibit the action of these channels in the nervous and cardiac organ systems. For instance, α-scorpion toxins MeuNaTxα-12 and MeuNaTxα-13 from Mesobuthus eupeus are neurotoxins that target voltage-gated Na+ channels (Navs), inhibiting fast inactivation. In vivo assays of MeuNaTxα-12 and MeuNaTxα-13 effects on mammalian and insect Navs show differential potency. These recombinants (MeuNaTxα-12 and (en)
name
  • Scorpion short toxin (en)
  • Scorpion long-chain toxin (en)
foaf:depiction
  • http://commons.wikimedia.org/wiki/Special:FilePath/scorpiontoxinproteinimage.png
  • http://commons.wikimedia.org/wiki/Special:FilePath/1agt.png
dcterms:subject
Wikipage page ID
Wikipage revision ID
Link from a Wikipage to another Wikipage
Link from a Wikipage to an external page
sameAs
TCDB
dbp:wikiPageUsesTemplate
thumbnail
PROSITE
  • PDOC00875 (en)
SCOP
caption
  • Agitoxin-2. Disulphide bonds are highlighted. PDB (en)
  • Crystal structure of toxin II from the scorpion Androctonus australis Hector. (en)
InterPro
  • IPR001947 (en)
  • IPR002061 (en)
Pfam
  • PF00451 (en)
  • PF00537 (en)
Pfam clan
  • CL0054 (en)
symbol
  • Toxin_2 (en)
  • Toxin_3 (en)
has abstract
  • Ein Skorpiontoxin ist ein Toxin, das von Skorpionen gebildet wird. (de)
  • Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal- or insect-specific and acts by binding with varying degrees of specificity to members of the Voltage-gated ion channel superfamily; specifically, voltage-gated sodium channels, voltage-gated potassium channels, and Transient Receptor Potential (TRP) channels. The result of this action is to activate or inhibit the action of these channels in the nervous and cardiac organ systems. For instance, α-scorpion toxins MeuNaTxα-12 and MeuNaTxα-13 from Mesobuthus eupeus are neurotoxins that target voltage-gated Na+ channels (Navs), inhibiting fast inactivation. In vivo assays of MeuNaTxα-12 and MeuNaTxα-13 effects on mammalian and insect Navs show differential potency. These recombinants (MeuNaTxα-12 and MeuNaTxα-13) exhibit their preferential affinity for mammalian and insect Na+ channels at the α-like toxins' active site, site 3, in order to inactivate the cell membrane depolarization faster[6]. The varying sensitivity of different Navs to MeuNaTxα-12 and MeuNaTxα-13 may be dependent on the substitution of a conserved Valine residue for a Phenylalanine residue at position 1630 of the LD4:S3-S4 subunit or due to various changes in residues in the LD4:S5-S6 subunit of the Navs. Ultimately, these actions can serve the purpose of warding off predators by causing pain (e.g., through the activation of sodium channels or TRP channels in sensory neurons) or to subdue predators (e.g., in the case of inhibition of cardiac ion channels). The family includes related short- and long-chain scorpion toxins. It also contains a group of proteinase inhibitors from the plants Arabidopsis thaliana and Brassica spp. The Brassica napus (oil seed rape) and Sinapis alba (white mustard) inhibitors, inhibit the catalytic activity of bovine beta-trypsin and bovine alpha-chymotrypsin, which belong to MEROPS peptidase family S1 (InterPro: IPR001254). This group of proteins is now used in the creation of insecticides, vaccines, and protein engineering scaffolds. (en)
OPM family
OPM protein
gold:hypernym
prov:wasDerivedFrom
page length (characters) of wiki page
Symbol
  • Toxin_2
  • Toxin_3
foaf:isPrimaryTopicOf
is Link from a Wikipage to another Wikipage of
Faceted Search & Find service v1.17_git139 as of Feb 29 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 08.03.3330 as of Mar 19 2024, on Linux (x86_64-generic-linux-glibc212), Single-Server Edition (378 GB total memory, 51 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software