2k10
From Proteopedia
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| - | + | ==Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif== | |
| - | + | <StructureSection load='2k10' size='340' side='right'caption='[[2k10]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2k10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rana_cascadae Rana cascadae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K10 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k10 OCA], [https://pdbe.org/2k10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k10 RCSB], [https://www.ebi.ac.uk/pdbsum/2k10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k10 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/RN2A_RANCS RN2A_RANCS] Antibacterial peptide with amphipathic alpha-helical structure. Active against E.coli ATCC 25726 (MIC=4-5 uM) and S.aureus ATCC 25923 (MIC=8-10 uM). Has a weak hemolytic activity on human erythrocytes (LC(50)=150-160 uM).<ref>PMID:17451843</ref> <ref>PMID:18387372</ref> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
Design of clinically valuable antibacterial agents based upon naturally occurring peptides requires the use of spectroscopic methods, particularly NMR, to determine the three-dimensional structure of the native peptide so that analogues with improved therapeutic properties can be made. Ranatuerin-2CSa (GILSSFKGVAKGVAKDLAG KLLETLKCKITGC), first isolated from skin secretions of the Cascades frog, Rana cascadae, represents a promising candidate for drug development. The peptide shows potent growth inhibitory activity against Escherichia coli (MIC=5 muM) and Staphylococcus aureus (MIC=10 muM) but displays haemolytic activity against human erythrocytes (LC(50)=160 muM). The solution structure of ranatuerin-2CSa was investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide lacks secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30) respectively. This structural information will facilitate the design of novel therapeutic agents based upon the ranatuerin-2CSa structure with improved antimicrobial potencies but decreased cytolytic activities against mammalian cells. | Design of clinically valuable antibacterial agents based upon naturally occurring peptides requires the use of spectroscopic methods, particularly NMR, to determine the three-dimensional structure of the native peptide so that analogues with improved therapeutic properties can be made. Ranatuerin-2CSa (GILSSFKGVAKGVAKDLAG KLLETLKCKITGC), first isolated from skin secretions of the Cascades frog, Rana cascadae, represents a promising candidate for drug development. The peptide shows potent growth inhibitory activity against Escherichia coli (MIC=5 muM) and Staphylococcus aureus (MIC=10 muM) but displays haemolytic activity against human erythrocytes (LC(50)=160 muM). The solution structure of ranatuerin-2CSa was investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide lacks secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30) respectively. This structural information will facilitate the design of novel therapeutic agents based upon the ranatuerin-2CSa structure with improved antimicrobial potencies but decreased cytolytic activities against mammalian cells. | ||
| - | + | Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif.,Subasinghage AP, Conlon JM, Hewage CM Biochim Biophys Acta. 2008 Jun;1784(6):924-9. Epub 2008 Mar 14. PMID:18387372<ref>PMID:18387372</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2k10" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rana cascadae]] |
| - | [[Category: | + | [[Category: Conlon M]] |
| - | [[Category: | + | [[Category: Hewage CM]] |
| - | [[Category: | + | [[Category: Subasinghage AP]] |
| - | + | ||
Current revision
Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif
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