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Solution Structure of CnErg1 (Ergtoxin), a HERG Specific Scorpion Toxin

Solution Structure of CnErg1 (Ergtoxin), a HERG Specific Scorpion Toxin

Allan M Torres, Paramjit Bansal, Paul F Alewood, Jane A Bursill, Philip W Kuchel, Jamie I Vandenberg

FEBS Lett. 2003 Mar 27;539(1-3):138-42.

PMID: 12650941

Abstract:

The three-dimensional structure of chemically synthesized CnErg1 (Ergtoxin), which specifically blocks HERG (human ether-a-go-go-related gene) K+ channels, was determined by nuclear magnetic resonance spectroscopy. CnErg1 consists of a triple-stranded beta-sheet and an alpha-helix, as is typical of K+ channel scorpion toxins. The peptide structure differs from the canonical structures in that the first beta-strand is shorter and is nearer to the second beta-strand rather than to the third beta-strand on the C-terminus. There is also a large hydrophobic patch on the surface of the toxin, surrounding a central lysine residue, Lys13. We postulate that this hydrophobic patch is likely to form part of the binding surface of the toxin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4246951	Ergtoxin from Centruroides noxius (Scorpion)			Price

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