- 関
- scorpion venom
WordNet
- a poisonous substance produced during the metabolism and growth of certain microorganisms and some higher plant and animal species
- arachnid of warm dry regions having a long segmented tail ending in a venomous stinger
PrepTutorEJDIC
- (特にバクテリアの)毒素
- サソリ
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/02/27 22:04:28」(JST)
[Wiki en表示]
| Scorpion long-chain toxin |
|
Crystal structure of toxin II from the scorpion Androctonus australis Hector.[1]
|
| Identifiers |
| Symbol |
Toxin_3 |
| Pfam |
PF00537 |
| InterPro |
IPR002061 |
| SCOP |
2sn3 |
| SUPERFAMILY |
2sn3 |
| OPM superfamily |
61 |
| OPM protein |
1djt |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
| Scorpion short toxin |
|
Agitoxin-2. Disulphide bonds are highlighted. PDB 1agt [2]
|
| Identifiers |
| Symbol |
Toxin_2 |
| Pfam |
PF00451 |
| Pfam clan |
CL0054 |
| InterPro |
IPR001947 |
| PROSITE |
PDOC00875 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal- or insect-specific and acts by binding to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission.
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,[3][4] inhibit the catalytic activity of bovine beta-trypsin and bovine alpha-chymotrypsin, which belong to MEROPS peptidase family S1 (InterPro: IPR001254).[5]
This group of proteins is now used in the creation of insecticides, vaccines, and protein engineering scaffolds.
Contents
- 1 Structure
- 2 Function
- 3 Subfamilies
- 4 References
- 5 External links
Structure
The complete covalent structure of several such toxins has been deduced: They comprise around 66 amino acid residues forming a three stranded anti-parallel beta sheet over which lies an alpha helix of approximately three turns. Four disulfide bridges cross-link the structure of the long-chain toxins whereas the short toxins contain only three.[6][7] BmKAEP, an anti-epilepsy peptide isolated from the venom of the Manchurian scorpion,[8] shows similarity to both scorpion neurotoxins and anti-insect toxins.
Function
The toxin's molecular function is to inhibit ion channels. Scorpion toxins are used in insecticides, vaccines, and protein engineering scaffolds. The toxins are now used to treat cancer patients by injecting fluorescent scorpion toxin into cancerous tissue to show tumor boundaries. Scorpion toxin genes are also used to kill insect pests by creating hypervirulent fungus in the insect through gene insertion.
Subfamilies
- Neurotoxin InterPro: IPR001219
References
- ^ PDB: 1PTX; Housset D; Habersetzer-Rochat C; Astier JP; Fontecilla-Camps JC (April 1994). "Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution". J. Mol. Biol. 238 (1): 88–103. doi:10.1006/jmbi.1994.1270. PMID 8145259.
- ^ Krezel, A. M.; Kasibhatla, C.; Hidalgo, P.; MacKinnon, R.; Wagner, G. (1995). "Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry". Protein Science. 4 (8): 1478–1489. doi:10.1002/pro.5560040805. PMC 2143198. PMID 8520473.
- ^ Ronchi S; Ceciliani F; Ascenzi P; Bortolotti F; Menegatti E; Palmieri S (1994). "Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seed". FEBS Lett. 342 (2): 221–224. doi:10.1016/0014-5793(94)80505-9. PMID 8143882.
- ^ Bolognesi M; Ronchi S; Tedeschi G; Ascenzi P; Bortolotti F; Menegatti E; Palmieri S; Thomas RM (1992). "Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seed". FEBS Lett. 301 (1): 10–14. doi:10.1016/0014-5793(92)80199-Q. PMID 1451776.
- ^ Rawlings ND; Barrett AJ; Tolle DP (2004). "Evolutionary families of peptidase inhibitors". Biochem. J. 378 (Pt 3): 705–16. doi:10.1042/BJ20031825. PMC 1224039. PMID 14705960.
- ^ Granier C; Kopeyan C; Rochat H; Mansuelle P; Sampieri F; Brando T; Bahraoui EM (1990). "Primary structure of scorpion anti-insect toxins isolated from the venom of Leiurus quinquestriatus quinquestriatus". FEBS Lett. 261 (2): 423–426. doi:10.1016/0014-5793(90)80607-K. PMID 2311768.
- ^ Rochat H; Gregoire J (1983). "Covalent structure of toxins I and II from the scorpion Buthus occitanus tunetanus". Toxicon. 21 (1): 153–162. doi:10.1016/0041-0101(83)90058-2. PMID 6845379.
- ^ Zhou XH; Yang D; Zhang JH; Liu CM; Lei KJ (1989). "Purification and N-terminal partial sequence of anti-epilepsy peptide from venom of the scorpion Buthus martensii Karsch". Biochem. J. 257 (2): 509–517. doi:10.1042/bj2570509. PMC 1135608. PMID 2930463.
External links
- Scorpion short toxins in PROSITE
- http://www.highbeam.com/doc/1G1-10342207.html
This article incorporates text from the public domain Pfam and InterPro IPR002061
UpToDate Contents
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English Journal
- A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif.
- Martin-Eauclaire MF1, Ferracci G1, Bosmans F2, Bougis PE3.
- The Journal of general physiology.J Gen Physiol.2015 Feb;145(2):155-62. doi: 10.1085/jgp.201411268.
- Animal toxins that inhibit voltage-gated sodium (Nav) channel fast inactivation can do so through an interaction with the S3b-S4 helix-turn-helix region, or paddle motif, located in the domain IV voltage sensor. Here, we used surface plasmon resonance (SPR), an optical approach that uses polarized l
- PMID 25624450
- Effects of Tityus serrulatus scorpion venom on thromboelastogram in rats.
- Lisboa TA1, Andrade MV2, Rezende-Neto JB3, Silva MJ4, Carvalho MG Jr1, Moraes-Santos T5, Ribeiro DD6, Cunha-Melo JR7.
- Toxicon : official journal of the International Society on Toxinology.Toxicon.2015 Feb;94:45-9. doi: 10.1016/j.toxicon.2014.10.010. Epub 2014 Nov 7.
- Thromboelastometry was used to evaluate blood coagulation in anesthetized rats after intravenous administration of Tityus serrulatus scorpion venom (Tx). Tracheostomy followed by catheterization of the left jugular vein and right carotid artery were performed for Tx or Ringer's lactate solution inje
- PMID 25449094
- Peptidomics combined with cDNA library unravel the diversity of centipede venom.
- Rong M1, Yang S1, Wen B2, Mo G3, Kang D1, Liu J1, Lin Z2, Jiang W4, Li B1, Du C2, Yang S5, Jiang H2, Feng Q6, Xu X2, Wang J7, Lai R8.
- Journal of proteomics.J Proteomics.2015 Jan 30;114:28-37. doi: 10.1016/j.jprot.2014.10.014. Epub 2014 Oct 29.
- Centipedes are one of the oldest venomous arthropods using toxin as their weapon to capture prey. But little attention was focused on them and only few centipede toxins were demonstrated with activity on ion channels. Therefore, more deep works are needed to understand the diversity of centipede ven
- PMID 25449838
Japanese Journal
- Potency of insect-specific scorpion toxins on mosquito control using Bacillus thuringiensis Cry4Aa(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)
- Synthesis and Characterization of κ-Hefutoxin 1 Analogs with Amino Acid Deletion
- Peptide science : proceedings of the ... Japanese Peptide Symposium 2012, 187-188, 2013-03-01
- NAID 10031161596
- Synthesis and Characterization of Spinoxin Analogs with Disulfide Bond Deletion
- Peptide science : proceedings of the ... Japanese Peptide Symposium 2012, 185-186, 2013-03-01
- NAID 10031161595
Related Links
- 2.2. Importance of scorpion toxins Scorpion toxins have already proven to be important pharmacological tools for probing the structure of the VGSC and studying the activation and inactivation processes that are a ...
- The structure of a complex containing a toxin bound to a potassium ion channel has been solved for the first time, revealing how scorpions have designed toxins that can recognize and target the filter that controls the ...
★リンクテーブル★
[★]
- 英
- scorpion toxin、scorpion venom
- 関
- α-サソリ毒、サソリ刺症
[★]
- 関
- alpha-scorpion toxin、scorpion toxin
[★]
αサソリ毒
- 関
- scorpion venom