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1ne5
From Proteopedia
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| - | [[Image:1ne5.jpg|left|200px]] | + | [[Image:1ne5.jpg|left|200px]] |
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| - | '''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1''' | + | {{Structure |
| + | |PDB= 1ne5 |SIZE=350|CAPTION= <scene name='initialview01'>1ne5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Strucuture of HERG Specific Scorpion Toxin CnErg1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NE5 is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12650941 12650941] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alewood, P.]] | [[Category: Alewood, P.]] | ||
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[[Category: triple-stranded beta-sheet]] | [[Category: triple-stranded beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:41 2008'' |
Revision as of 10:55, 20 March 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
Page seeded by OCA on Thu Mar 20 12:55:41 2008
