Title |
Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin
|
---|---|
Published in |
Febs Letters, March 2003
|
DOI | 10.1016/s0014-5793(03)00216-3 |
Pubmed ID | |
Authors |
Allan M Torres, Paramjit Bansal, Paul F Alewood, Jane A Bursill, Philip W Kuchel, Jamie I Vandenberg |
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. |
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