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BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian scorpion Buthus tamulus

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Title BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian scorpion Buthus tamulus
 
Creator DHAWAN, R
VARSHNEY, A
MATHEW, MK
LALA, AK
 
Subject ca2+-activated k+ channels
magnetic-resonance spectroscopy
3-dimensional structure
receptor-sites
toxin
peptides
venom
charybdotoxin
affinity
blocker
scorpion
toxin
homology
voltage-gated potassium channel
patch clamp
buthus tamulus
 
Description A novel inhibitor of voltage-gated potassium channel was isolated and purified to homogeneity from the venom of the red scorpion Buthus tamulus. The primary sequence of this toxin, named BTK-2, as determined by peptide sequencing shows that it has 32 amino acid residues with six conserved cysteines. The molecular weight of the toxin was found to be 3452 Da. It was found to block the human potassium channel hKv1.1 (IC50 = 4.6 muM). BTK-2 shows 40-70% sequence similarity to the family of the short-chain toxins that specifically block potassium channels. Multiple sequence alignment helps to categorize the toxin in the ninth subfamily of the K+ channel blockers. The modeled structure of BTK-2 shows an alpha/beta scaffold similar to those of the other short scorpion toxins. Comparative analysis of the structure with those of the other toxins helps to identify the possible structure-function relationship that leads to the difference in the specificity of BTK-2 from that of the other scorpion toxins. The toxin can also be used to study the assembly of the hKv1.1 channel. (C) 2003 Federation of European Biochemical Societies. .
 
Publisher ELSEVIER SCIENCE BV
 
Date 2011-07-24T11:34:02Z
2011-12-26T12:53:18Z
2011-12-27T05:40:35Z
2011-07-24T11:34:02Z
2011-12-26T12:53:18Z
2011-12-27T05:40:35Z
2003
 
Type Article
 
Identifier FEBS LETTERS, 539(40603), 7-13
0014-5793
http://dx.doi.org/10.1016/S0014-5793(03)00125-X
http://dspace.library.iitb.ac.in/xmlui/handle/10054/6412
http://hdl.handle.net/10054/6412
 
Language en