5ipo

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m (Protected "5ipo" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5ipo is ON HOLD
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==Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi==
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<StructureSection load='5ipo' size='340' side='right' caption='[[5ipo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ipo]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IPO FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ipo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ipo OCA], [http://pdbe.org/5ipo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ipo RCSB], [http://www.ebi.ac.uk/pdbsum/5ipo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ipo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/KBX3_HADGE KBX3_HADGE]] Hge-scorpine has antibacterial activity against B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic activities.<ref>PMID:18030427</ref> Hge36 peptide blocks Kv1.1/KCNA1 (IC(50)=185 nM) potassium channels. Shows a weak hemolytic activity.<ref>PMID:18030427</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Scorpine-like peptides are two domain peptides found in different scorpion venoms displaying various antimicrobial, cytolytic, and potassium channel-blocking activities. The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine-like peptide from the venom of Hoffmannihadrurus gertschi. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel-blocking and antiparasitic activities. Our results are important to rationalize the structure-function relationships of a pharmacologically versatile molecular scaffold.
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Authors: Flores-Solis, D., Rodriguez De La Vega, R., del Rio-Portilla, F.
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Solution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi.,Flores-Solis D, Toledano Y, Rodriguez-Lima O, Cano-Sanchez P, Ramirez-Cordero BE, Landa A, Rodriguez de la Vega RC, Del Rio-Portilla F FEBS Lett. 2016 Jun 17. doi: 10.1002/1873-3468.12255. PMID:27314815<ref>PMID:27314815</ref>
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Description: Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Rodriguez De La Vega, R]]
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<div class="pdbe-citations 5ipo" 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: Flores-Solis, D]]
[[Category: Flores-Solis, D]]
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[[Category: Del Rio-Portilla, F]]
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[[Category: Rio-Portilla, F del]]
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[[Category: Vega, R Rodriguez De La]]
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[[Category: Antiparasitic activity]]
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[[Category: Hadrurus gertschi]]
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[[Category: Scorpine-like peptide]]
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[[Category: Toxin]]

Revision as of 10:25, 13 July 2016

Solution Structure of Hge36: Scorpine-like Peptide from Hadrurus Gertschi

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