Premium
Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin
Author(s) -
Torres Allan M,
Bansal Paramjit,
Alewood Paul F,
Bursill Jane A,
Kuchel Philip W,
Vandenberg Jamie I
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00216-3
Subject(s) - scorpion toxin , herg , chemistry , scorpion , toxin , stereochemistry , peptide , biophysics , crystallography , biochemistry , potassium channel , biology , venom
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.