1ne5
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ne5 OCA], [http://www.ebi.ac.uk/pdbsum/1ne5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ne5 RCSB]</span> | ||
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[[Category: triple-stranded beta-sheet]] | [[Category: triple-stranded beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:06 2008'' |
Revision as of 19:29, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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