2l5r

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==Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C==
==Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C==
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<StructureSection load='2l5r' size='340' side='right'caption='[[2l5r]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l5r' size='340' side='right'caption='[[2l5r]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l5r]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alytes_obstetricans Alytes obstetricans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5R FirstGlance]. <br>
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</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=2l5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5r OCA], [https://pdbe.org/2l5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5r RCSB], [https://www.ebi.ac.uk/pdbsum/2l5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5r ProSAT]</span></td></tr>
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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</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=2l5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5r OCA], [https://pdbe.org/2l5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5r RCSB], [https://www.ebi.ac.uk/pdbsum/2l5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5r ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ATI1C_ALYOB ATI1C_ALYOB] Antibacterial peptide with amphipathic alpha-helical structure that shows selective growth-inhibitory activity against Gram-negative bacteria but low hemolytic activity against human erythrocytes (LC(50)=145-220 uM) (PubMed:19463738, PubMed:21565166). It is moderately active against the Gram-negative bacteria E.coli (MIC=25 uM), K.pneumoniae (MIC=50 uM), P.aeruginosa (MIC=25 uM), A.baumannii (MIC=6 uM), and is weaky active against the Gram-positive S.aureus (MIC=100-250 uM) (PubMed:19463738, PubMed:21565166).<ref>PMID:19463738</ref> <ref>PMID:21565166</ref>
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Alyteserin-1c (GLKEIFKAGLGSLVKGIAAHVAS.NH(2)), first isolated from skin secretions of the midwife toad Alytes obstetricans, shows selective growth-inhibitory activity against Gram-negative bacteria. The structures of alyteserin-1c and its more potent and less haemolytic analogue [E4K]alyteserin-1c were investigated in various solution and membrane mimicking environments by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide displays a lack of secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by an extended alpha helix between residues Leu(2) and Val(21). Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21). Positional studies of the peptides in SDS, DPC and DHPC media show that the N-terminal and central residues lie inside the micelle while C-terminal residues beyond Ala(19) do not interact with the micelles.
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Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.,Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM Biochim Biophys Acta. 2011 Aug;1808(8):1975-84. Epub 2011 Apr 30. PMID:21565166<ref>PMID:21565166</ref>
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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 2l5r" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alytes obstetricans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Conlon, M]]
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[[Category: Conlon M]]
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[[Category: Hewage, C M]]
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[[Category: Hewage CM]]
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[[Category: Subasinghage, A P]]
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[[Category: Subasinghage AP]]
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[[Category: Alpha helix]]
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[[Category: Antimicrobial protein]]
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Current revision

Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C

PDB ID 2l5r

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