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- Title
Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin
- Authors
Torres, Allan M.; Bansal, Paramjit; Alewood, Paul F.; Bursill, Jane A.; Kuchel, Philip W.; Vandenberg, Jamie I.
- 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 β-sheet and an α-helix, as is typical of K+ channel scorpion toxins. The peptide structure differs from the canonical structures in that the first β-strand is shorter and is nearer to the second β-strand rather than to the third β-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.
- Subjects
GENES; NUCLEAR magnetic resonance spectroscopy
- Publication
FEBS Letters, 2003, Vol 539, Issue 1-3, p138
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)00216-3