1ne5
From Proteopedia
(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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| - | [[Image:1ne5.jpg|left|200px]]<br /><applet load="1ne5" size=" | + | [[Image:1ne5.jpg|left|200px]]<br /><applet load="1ne5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ne5" /> | caption="1ne5" /> | ||
'''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1'''<br /> | '''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of chemically synthesized CnErg1 | + | 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== | ==About this Structure== | ||
| - | 1NE5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1NE5 is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alewood, P.]] | [[Category: Alewood, P.]] | ||
| - | [[Category: Kuchel, P | + | [[Category: Kuchel, P W.]] |
[[Category: Paramjit, B.]] | [[Category: Paramjit, B.]] | ||
| - | [[Category: Torres, A | + | [[Category: Torres, A M.]] |
| - | [[Category: Vandenberg, J | + | [[Category: Vandenberg, J I.]] |
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
[[Category: triple-stranded beta-sheet]] | [[Category: triple-stranded beta-sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:09 2008'' |
Revision as of 12:05, 21 February 2008
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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
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