Scyllatoxin

Scyllatoxin
	according to PDB 1SCY
other names	Leiurotoxin I, LeTx I, Potassium channel toxin alpha-KTx 5.1
Mass / length primary structure	31 amino acids , 3,430 Da
Identifier
External IDs	UniProt : P16341 ;
Occurrence
Parent taxon	Leiurus quinquestriatus

Scyllatoxin (synonymous potassium channel toxin alpha-KTx 5.1 , leiurotoxin I ) is a neurotoxin from the scorpion Leiurus quinquestriatus hebraeus (yellow Mediterranean scorpion ).

properties

Scyllatoxin is a protein and scorpion toxin . It binds and inhibits calcium- activated potassium channels (type SK-Ca, also known as apamin -sensitive potassium channels), but not hSK3 ex4 . Scyllatoxin is not structurally related to apamin. Scyllatoxin is amidated and has three disulfide bridges between C 8: C26, C12: C28 and C3: C21. Arginines at positions 6 and 13 are essential for binding and effect. Scyllatoxin only makes up 0.02% of the protein mass in scorpion venom.

Web links

MeSH scyllatoxin

Individual evidence

^ OH Wittekindt, V. Visan, H. Tomita, F. Imtiaz, JJ Gargus, F. Lehmann-Horn, S. Grissmer, DJ Morris-Rosendahl: An apamin- and scyllatoxin-insensitive isoform of the human SK3 channel. In: Molecular pharmacology. Volume 65, Number 3, March 2004, pp. 788-801, doi : 10.1124 / mol.65.3.788 , PMID 14978258 .
↑ GG Chicchi, G. Gimenez-Gallego, E. Ber, ML Garcia, R. Winquist, MA Cascieri: Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom. In: The Journal of biological chemistry. Volume 263, Number 21, July 1988, pp. 10192-10197, PMID 2839478 .
↑ JM Sabatier, C. Lecomte, K. Mabrouk, H. Darbon, R. Oughideni, S. Canarelli, H. Rochat, MF Martin-Eauclaire, J. van Rietschoten: Synthesis and characterization of leiurotoxin I analogs lacking one disulfide bridge: evidence that disulfide pairing 3-21 is not required for full toxin activity. In: Biochemistry. Volume 35, Number 33, August 1996, pp. 10641-10647, doi : 10.1021 / bi960533d , PMID 8718853 .
↑ E. Buisine, JM Wieruszeski, G. Lippens, D. Wouters, A. Tartar, P. SAUTIERE: Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1 H-NMR structure of leiuropeptide II. In: The journal of peptide research: official journal of the American Peptide Society. Volume 49, Number 6, June 1997, pp. 545-555, PMID 9266482 .
↑ Q. Zhu, S. Liang, L. Martin, S. Gasparini, A. Ménez, C. Vita: Role of disulfide bonds in folding and activity of leiurotoxin I: just two disulfides suffice. In: Biochemistry. Volume 41, Number 38, September 2002, pp. 11488-11494, PMID 12234192 .

[1] OH Wittekindt, V. Visan, H. Tomita, F. Imtiaz, JJ Gargus, F. Lehmann-Horn, S. Grissmer, DJ Morris-Rosendahl: An apamin- and scyllatoxin-insensitive isoform of the human SK3 channel. In: Molecular pharmacology. Volume 65, Number 3, March 2004, pp. 788-801, doi : 10.1124 / mol.65.3.788 , PMID 14978258 .

[2] GG Chicchi, G. Gimenez-Gallego, E. Ber, ML Garcia, R. Winquist, MA Cascieri: Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom. In: The Journal of biological chemistry. Volume 263, Number 21, July 1988, pp. 10192-10197, PMID 2839478 .

[3] JM Sabatier, C. Lecomte, K. Mabrouk, H. Darbon, R. Oughideni, S. Canarelli, H. Rochat, MF Martin-Eauclaire, J. van Rietschoten: Synthesis and characterization of leiurotoxin I analogs lacking one disulfide bridge: evidence that disulfide pairing 3-21 is not required for full toxin activity. In: Biochemistry. Volume 35, Number 33, August 1996, pp. 10641-10647, doi : 10.1021 / bi960533d , PMID 8718853 .

[4] E. Buisine, JM Wieruszeski, G. Lippens, D. Wouters, A. Tartar, P. SAUTIERE: Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1 H-NMR structure of leiuropeptide II. In: The journal of peptide research: official journal of the American Peptide Society. Volume 49, Number 6, June 1997, pp. 545-555, PMID 9266482 .

[5] Q. Zhu, S. Liang, L. Martin, S. Gasparini, A. Ménez, C. Vita: Role of disulfide bonds in folding and activity of leiurotoxin I: just two disulfides suffice. In: Biochemistry. Volume 41, Number 38, September 2002, pp. 11488-11494, PMID 12234192 .