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

Torres, A. M., Bansal, P., Alewood, P. F., Bursill, J. A., Kuchel, P. W. and Vandenberg, J. I. (2003) Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin. Febs Letters, 539 1-3: 138-142. doi:10.1016/S0014-5793(03)00216-3

Author Torres, A. M.
Bansal, P.
Alewood, P. F.
Bursill, J. A.
Kuchel, P. W.
Vandenberg, J. I.
Title Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin
Journal name Febs Letters   Check publisher's open access policy
ISSN 0014-5793
Publication date 2003-03-27
Sub-type Article (original research)
DOI 10.1016/S0014-5793(03)00216-3
Volume 539
Issue 1-3
Start page 138
End page 142
Total pages 5
Editor Stuart Ferguson
Place of publication Netherlands
Publisher Elsevier BV
Collection year 2003
Language eng
Subject C1
270100 Biochemistry and Cell Biology
780103 Chemical sciences
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 a-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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Keyword Biochemistry & Molecular Biology
Cell Biology
Human Ether-a-go-go-related Gene
K+ Ion Channel
Chemical Synthesis
Nmr Structure
K+ Channels
Potassium Channel
Biological Macromolecules
Noesy Spectra
Q-Index Code C1

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Created: Wed, 15 Aug 2007, 01:41:13 EST