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

FEBS Letters

Bursill, Jane A³  Torres, Allan M¹  Bansal, Paramjit²  Kuchel, Philip W¹  Alewood, Paul F²  Vandenberg, Jamie I³ 

[1] School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia;Institute for Molecular Bioscience, University of Queensland, St. Lucia, Qld 4072, Australia;Victor Chang Cardiac Research Institute and Department of Medicine, University of New South Wales, 384 Victoria Street, Darlinghurst, NSW 2010, Australia

关键词: Ergtoxin;    Human ether-a-go-go-related gene;    K+ ion channel;    Chemical synthesis;    NMR structure;    HERG;    human ether-a-go-go-related gene;    NOESY;    nuclear Overhauser enhancement spectroscopy;    rmsd;    root-mean-square deviation;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/S0014-5793(03)00216-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown