2h9x

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(New page: 200px<br /><applet load="2h9x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h9x" /> '''NMR structure for the CgNa toxin from the se...)
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[[Image:2h9x.jpg|left|200px]]<br /><applet load="2h9x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h9x" />
 
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'''NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea'''<br />
 
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==Overview==
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==NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea==
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CgNa is a toxin from the sea anemone Condylactis gigantea that is, comprised of 47-residues. The structure of CgNa, solved by 1H NMR, spectroscopy, is somewhat atypical, displaying significant homologies to, both type I and II anemonae toxins, as well as a considerable number of, exceptions to what are considered as canonical structural elements of this, group of toxins, and that are thought to be essential for their activity., Furthermore, unique residues in CgNa define a characteristic structure, with strong negatively charged surface-patches. These patches disrupt a, surface-exposed cluster of hydrophobic residues present in all the toxins, described in this group to date. A thorough characterization by, patch-clamp using rat dorsal root ganglion neurons indicate that CgNa, preferentially binds to TTX-S Na + channels in the resting state. This, association increases the inactivation time constant and the rate of, recovery from inactivation, inducing a significant shift to the left in, the steady state of the inactivation curve. The specific structural, features of CgNa may explain its weaker inhibitory capacity when compared, to the other type I and II anemone toxins.
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<StructureSection load='2h9x' size='340' side='right'caption='[[2h9x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Condylactis_gigantea Condylactis gigantea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H9X FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9x OCA], [https://pdbe.org/2h9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9x RCSB], [https://www.ebi.ac.uk/pdbsum/2h9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/TXNA_CONGI TXNA_CONGI]] Slows down the inactivation process of TTX-sensitive voltage-gated sodium channels (Nav). Has a strong crab-paralyzing activity.<ref>PMID:16814340</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/2h9x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2h9x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CgNa (Condylactis gigantea neurotoxin) is a 47-amino-acid- residue toxin from the giant Caribbean sea anemone Condylactis gigantea. The structure of CgNa, which was solved by 1H-NMR spectroscopy, is somewhat atypical and displays significant homology with both type I and II anemone toxins. CgNa also displays a considerable number of exceptions to the canonical structural elements that are thought to be essential for the activity of this group of toxins. Furthermore, unique residues in CgNa define a characteristic structure with strong negatively charged surface patches. These patches disrupt a surface-exposed cluster of hydrophobic residues present in all anemone-derived toxins described to date. A thorough characterization by patch-clamp analysis using rat DRG (dorsal root ganglion) neurons indicated that CgNa preferentially binds to TTX-S (tetrodotoxin-sensitive) voltage-gated sodium channels in the resting state. This association increased the inactivation time constant and the rate of recovery from inactivation, inducing a significant shift in the steady state of inactivation curve to the left. The specific structural features of CgNa may explain its weaker inhibitory capacity when compared with the other type I and II anemone toxins.
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==About this Structure==
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CgNa, a type I toxin from the giant Caribbean sea anemone Condylactis gigantea shows structural similarities to both type I and II toxins, as well as distinctive structural and functional properties(1).,Salceda E, Perez-Castells J, Lopez-Mendez B, Garateix A, Salazar H, Lopez O, Aneiros A, Standker L, Beress L, Forssmann WG, Soto E, Jimenez-Barbero J, Gimenez-Gallego G Biochem J. 2007 Aug 15;406(1):67-76. PMID:17506725<ref>PMID:17506725</ref>
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2H9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Condylactis_gigantea Condylactis gigantea]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H9X OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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CgNa, a type I toxin from the sea anemone Condylactis gigantea shows structural similarities to both type I and II toxins, as well as distinctive structural and functional properties., Salceda E, Perez-Castells J, Lopez-Mendez B, Garateix A, Salazar H, Lopez O, Aneiros A, Standker L, Beress L, Forssmann WG, Soto E, Jimenez-Barbero J, Gimenez-Gallego G, Biochem J. 2007 May 16;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17506725 17506725]
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</div>
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<div class="pdbe-citations 2h9x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Condylactis gigantea]]
[[Category: Condylactis gigantea]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gimenez-Gallego, G.]]
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[[Category: Gimenez-Gallego, G]]
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[[Category: Jimenez-Barbero, J.]]
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[[Category: Jimenez-Barbero, J]]
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[[Category: Lopez-Mendez, B.]]
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[[Category: Lopez-Mendez, B]]
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[[Category: Perez-Castells, J.]]
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[[Category: Perez-Castells, J]]
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[[Category: beta sheet]]
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[[Category: Beta sheet]]
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[[Category: Toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:37:50 2007''
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Current revision

NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea

PDB ID 2h9x

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