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1ne5
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(New page: 200px<br /><applet load="1ne5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ne5" /> '''Solution Strucuture of HERG Specific Scorpio...)
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Revision as of 20:03, 20 November 2007
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Solution Strucuture of HERG Specific Scorpion Toxin CnErg1
Overview
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.
About this Structure
1NE5 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin., Torres AM, Bansal P, Alewood PF, Bursill JA, Kuchel PW, Vandenberg JI, FEBS Lett. 2003 Mar 27;539(1-3):138-42. PMID:12650941
Page seeded by OCA on Tue Nov 20 22:10:50 2007
