1ne5: Difference between revisions

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[[Image:1ne5.~~jpg~~|left|200px]]

[[Image:1ne5.png|left|200px]]

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~~'''~~Solution Strucuture of HERG Specific Scorpion Toxin CnErg1~~'''~~

===Solution Strucuture of HERG Specific Scorpion Toxin CnErg1===

~~==Overview==~~

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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 line below this paragraph, {{ABSTRACT_PUBMED_12650941}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12650941 is the PubMed ID number.

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==About this Structure==

1NE5 is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].

1NE5 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].

==Reference==

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[[Category: Alpha-helix]]

[[Category: Triple-stranded beta-sheet]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:25:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:25:49 2008''

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-[[Image:1ne5.jpg|left|200px]]
+{{Seed}}
+[[Image:1ne5.png|left|200px]]
 <!--
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 {{STRUCTURE_1ne5|  PDB=1ne5  |  SCENE=  }}
-'''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12650941}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12650941 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12650941}}
 ==About this Structure==
-NE5 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].
+NE5 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA].
 ==Reference==
@@ Line 28: / Line 32: @@
 [[Category: Alpha-helix]]
 [[Category: Triple-stranded beta-sheet]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:25:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:25:49 2008''