Charybdotoxin a

Charybdotoxin a
	according to PDB 2CRD
other names	ChTX-Lq1, ChTx-a, Potassium channel toxin alpha-KTx 1.1
	Existing structure data : PDB 1BAH , PDB 1CMR , PDB 2A9H
Mass / length primary structure	37 amino acids
Precursor	59 amino acids, 6,674 Da
Identifier
External IDs	UniProt : P13487 ;

Charybdotoxin a (synonym potassium channel toxin alpha-KTx 1.1 ) is a neurotoxin from the yellow Mediterranean scorpion Leiurus quinquestriatus hebraeus .

properties

Charybdotoxin a is a peptide and a scorpion toxin from the venom of Leiurus quinquestriatus hebraeus , as is Charybdotoxin b . It binds and inhibits the potassium channels of the maxi-K group and the calcium-dependent potassium channels KCa1.1 / KCNMA1 and others as well as the voltage-gated potassium channels Kv1.3 / KCNA3 , Kv1.2 / KCNA2 , Kv1.6 / KCNA3 and to a lesser extent Shaker / Sh , but not Kv1.1 / KCNA1 , Kv1.5 / KCNA5 , Kv2.1 / KCNB1 , Kv3.1 / KCNC1 and Kv11.1 / KCNH2 / ERG1 . Charybdotoxin a has a pyrrolidone carboxylic acid . It is structurally related to iberiotoxin , limbatus toxin and also to noxious toxin , margatoxin and tityus toxin Kα .

Web links

MeSH Charybdotoxin a

Individual evidence

↑ K. Lucchesi, A. Ravindran, H. Young, E. Moczydlowski: Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2 + -activated K + channels. In: The Journal of membrane biology. Volume 109, Number 3, August 1989, pp. 269-281, PMID 2477548 .
↑ ML Garcia, M. Garcia-Calvo, P. Hidalgo, A. Lee, R. MacKinnon: Purification and characterization of three inhibitors of voltage-dependent K + channels from Leiurus quinquestriatus var. Hebraeus venom. In: Biochemistry. Volume 33, Number 22, June 1994, pp. 6834-6839, PMID 8204618 .
↑ S. Grissmer, AN Nguyen, J. Aiyar, DC Hanson, RJ Mather, GA Gutman, MJ Karmilowicz, DD Auperin, KG Chandy: Pharmacological characterization of five cloned voltage-gated K + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. In: Molecular pharmacology. Volume 45, Number 6, June 1994, pp. 1227-1234, PMID 7517498 .
↑ M. Zhang, YV Korolkova, J. Liu, M. Jiang, EV Grishin, GN Tseng: BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. In: Biophysical Journal. Volume 84, number 5, May 2003, pp. 3022-3036, doi : 10.1016 / S0006-3495 (03) 70028-9 , PMID 12719233 , PMC 1302864 (free full text).
^ Hervé Rochat: Animal Toxins. Springer Science & Business Media, 2000, ISBN 978-3-764-35983-6 , p. 184.

[1] K. Lucchesi, A. Ravindran, H. Young, E. Moczydlowski: Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2 + -activated K + channels. In: The Journal of membrane biology. Volume 109, Number 3, August 1989, pp. 269-281, PMID 2477548 .

[2] ML Garcia, M. Garcia-Calvo, P. Hidalgo, A. Lee, R. MacKinnon: Purification and characterization of three inhibitors of voltage-dependent K + channels from Leiurus quinquestriatus var. Hebraeus venom. In: Biochemistry. Volume 33, Number 22, June 1994, pp. 6834-6839, PMID 8204618 .

[3] S. Grissmer, AN Nguyen, J. Aiyar, DC Hanson, RJ Mather, GA Gutman, MJ Karmilowicz, DD Auperin, KG Chandy: Pharmacological characterization of five cloned voltage-gated K + channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. In: Molecular pharmacology. Volume 45, Number 6, June 1994, pp. 1227-1234, PMID 7517498 .

[4] M. Zhang, YV Korolkova, J. Liu, M. Jiang, EV Grishin, GN Tseng: BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. In: Biophysical Journal. Volume 84, number 5, May 2003, pp. 3022-3036, doi : 10.1016 / S0006-3495 (03) 70028-9 , PMID 12719233 , PMC 1302864 (free full text).

[Rochat-5] Hervé Rochat: Animal Toxins. Springer Science & Business Media, 2000, ISBN 978-3-764-35983-6 , p. 184.