1ne5

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[[Image:1ne5.jpg|left|200px]]
[[Image:1ne5.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ne5", creates the "Structure Box" on the page.
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{{STRUCTURE_1ne5| PDB=1ne5 | SCENE= }}
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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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'''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==
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1NE5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].
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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.]]
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[[Category: alpha-helix]]
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[[Category: Alpha-helix]]
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[[Category: triple-stranded beta-sheet]]
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[[Category: Triple-stranded beta-sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:25:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:06 2008''
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Revision as of 23:25, 2 May 2008

Template:STRUCTURE 1ne5

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

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