2k10: Difference between revisions
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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k10]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K10 FirstGlance]. <br> | |||
</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=2k10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k10 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k10 RCSB], [http://www.ebi.ac.uk/pdbsum/2k10 PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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> | |||
[[Category: Conlon, M | == References == | ||
[[Category: Hewage, C M | <references/> | ||
[[Category: Subasinghage, A P | __TOC__ | ||
</StructureSection> | |||
[[Category: Conlon, M]] | |||
[[Category: Hewage, C M]] | |||
[[Category: Subasinghage, A P]] | |||
[[Category: Antimicrobial peptide]] | [[Category: Antimicrobial peptide]] | ||
[[Category: Antimicrobial protein]] | [[Category: Antimicrobial protein]] | ||
Revision as of 18:27, 21 December 2014
Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif
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