1ne5: Difference between revisions
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{{STRUCTURE_1ne5| PDB=1ne5 | SCENE= }} | |||
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'''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1''' | '''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1''' | ||
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==About this Structure== | ==About this Structure== | ||
1NE5 is a [[Single protein]] structure | 1NE5 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Torres, A M.]] | [[Category: Torres, A M.]] | ||
[[Category: Vandenberg, J I.]] | [[Category: Vandenberg, J I.]] | ||
[[Category: | [[Category: Alpha-helix]] | ||
[[Category: | [[Category: Triple-stranded beta-sheet]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:25:20 2008'' | |||
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Revision as of 23:25, 2 May 2008
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. 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 Sat May 3 02:25:20 2008
