1ne5
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Solution Structure of HERG Specific Scorpion Toxin CnErg1== | |
| - | + | <StructureSection load='1ne5' size='340' side='right' caption='[[1ne5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1ne5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NE5 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1ne5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ne5 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1ne5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:12650941</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Potassium channel toxin|Potassium channel toxin]] | *[[Potassium channel toxin|Potassium channel toxin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Alewood, P.]] | [[Category: Alewood, P.]] | ||
[[Category: Kuchel, P W.]] | [[Category: Kuchel, P W.]] | ||
Revision as of 16:07, 29 September 2014
Solution Structure of HERG Specific Scorpion Toxin CnErg1
| |||||||||||
