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| - | {{Seed}} | |
| - | [[Image:2k10.png|left|200px]] | |
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| - | <!--
| + | ==Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif== |
| - | The line below this paragraph, containing "STRUCTURE_2k10", creates the "Structure Box" on the page.
| + | <StructureSection load='2k10' size='340' side='right'caption='[[2k10]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <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> |
| - | or leave the SCENE parameter empty for the default display.
| + | </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> |
| - | {{STRUCTURE_2k10| PDB=2k10 | SCENE= }}
| + | </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. |
| | | | |
| - | ===Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif===
| + | 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> |
| | | | |
| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_18387372}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 2k10" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 18387372 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_18387372}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | 2K10 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K10 OCA].
| + | [[Category: Rana cascadae]] |
| - | | + | [[Category: Conlon M]] |
| - | ==Reference== | + | [[Category: Hewage CM]] |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18387372 18387372]
| + | [[Category: Subasinghage AP]] |
| - | [[Category: Single protein]] | + | |
| - | [[Category: Conlon, M.]] | + | |
| - | [[Category: Hewage, C M.]] | + | |
| - | [[Category: Subasinghage, A P.]] | + | |
| - | [[Category: Antimicrobial peptide]] | + | |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Molecular modelling]]
| + | |
| - | [[Category: Nmr]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:08:37 2008''
| + | |
| Structural highlights
Function
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).[1] [2]
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Conlon JM, Al-Dhaheri A, Al-Mutawa E, Al-Kharrge R, Ahmed E, Kolodziejek J, Nowotny N, Nielsen PF, Davidson C. Peptide defenses of the Cascades frog Rana cascadae: implications for the evolutionary history of frogs of the Amerana species group. Peptides. 2007 Jun;28(6):1268-74. PMID:17451843 doi:10.1016/j.peptides.2007.03.010
- ↑ Subasinghage AP, Conlon JM, Hewage CM. Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif. Biochim Biophys Acta. 2008 Jun;1784(6):924-9. Epub 2008 Mar 14. PMID:18387372 doi:http://dx.doi.org/S1570-9639(08)00078-2
- ↑ Subasinghage AP, Conlon JM, Hewage CM. Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif. Biochim Biophys Acta. 2008 Jun;1784(6):924-9. Epub 2008 Mar 14. PMID:18387372 doi:http://dx.doi.org/S1570-9639(08)00078-2
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