2m6a

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'''Unreleased structure'''
 
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The entry 2m6a is ON HOLD until Paper Publication
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==NMR spatial structure of the antimicrobial peptide Tk-Amp-X2==
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<StructureSection load='2m6a' size='340' side='right'caption='[[2m6a]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2m6a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare_subsp._vulgare Hordeum vulgare subsp. vulgare]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M6A FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2m6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m6a OCA], [https://pdbe.org/2m6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m6a RCSB], [https://www.ebi.ac.uk/pdbsum/2m6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m6a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F2EGM1_HORVV F2EGM1_HORVV]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In this study, we present the spatial structure of the wheat antimicrobial peptide (AMP) Tk-AMP-X2 studied using NMR spectroscopy. This peptide was found to adopt a disulfide-stabilized alpha-helical hairpin fold and therefore belongs to the alpha-hairpinin family of plant defense peptides. Based on Tk-AMP-X2 structural similarity to cone snail and scorpion potassium channel blockers, a mutant molecule, Tk-hefu, was engineered by incorporating the functionally important residues from kappa-hefutoxin 1 onto the Tk-AMP-X2 scaffold. The designed peptide contained the so-called essential dyad of amino acid residues significant for channel-blocking activity. Electrophysiological studies showed that although the parent peptide Tk-AMP-X2 did not present any activity against potassium channels, Tk-hefu blocked Kv1.3 channels with similar potency (IC50 approximately 35 mum) to kappa-hefutoxin 1 (IC50 approximately 40 mum). We conclude that alpha-hairpinins are attractive in their simplicity as structural templates, which may be used for functional engineering and drug design.
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Authors: Usmanova, D.R., Mineev, K.S., Arseniev, A.S., Berkut, A.A., Oparin, P.B., Grishin, E.V., Vassilevski, A.A.
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Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design.,Berkut AA, Usmanova DR, Peigneur S, Oparin PB, Mineev KS, Odintsova TI, Tytgat J, Arseniev AS, Grishin EV, Vassilevski AA J Biol Chem. 2014 May 16;289(20):14331-40. doi: 10.1074/jbc.M113.530477. Epub, 2014 Mar 26. PMID:24671422<ref>PMID:24671422</ref>
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Description: NMR spatial structure of the antimicrobial peptide Tk-Amp-X2
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2m6a" 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>
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[[Category: Hordeum vulgare subsp. vulgare]]
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[[Category: Large Structures]]
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[[Category: Arseniev AS]]
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[[Category: Berkut AA]]
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[[Category: Grishin EV]]
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[[Category: Mineev KS]]
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[[Category: Oparin PB]]
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[[Category: Usmanova DR]]
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[[Category: Vassilevski AA]]

Current revision

NMR spatial structure of the antimicrobial peptide Tk-Amp-X2

PDB ID 2m6a

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