1ne5: Difference between revisions

New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[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, (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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].  
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.W.]]
[[Category: Kuchel, P W.]]
[[Category: Paramjit, B.]]
[[Category: Paramjit, B.]]
[[Category: Torres, A.M.]]
[[Category: Torres, A M.]]
[[Category: Vandenberg, J.I.]]
[[Category: Vandenberg, J I.]]
[[Category: alpha-helix]]
[[Category: alpha-helix]]
[[Category: triple-stranded beta-sheet]]
[[Category: triple-stranded beta-sheet]]


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