Referenced in: none

Automatically associated channels: Kir2.3 , Kv11.1

Title: Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin.

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

Journal, date & volume: FEBS Lett., 2003 Mar 27 , 539, 138-42

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/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.