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| | ==NMR structures of hylin-a1 analogs: Hylin-Ac== | | ==NMR structures of hylin-a1 analogs: Hylin-Ac== |
| - | <StructureSection load='5j6t' size='340' side='right'caption='[[5j6t]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5j6t' size='340' side='right'caption='[[5j6t]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j6t]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J6T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Boana_albopunctata Boana albopunctata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J6T FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j6w|5j6w]], [[5j6v|5j6v]]</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=5j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6t OCA], [https://pdbe.org/5j6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j6t RCSB], [https://www.ebi.ac.uk/pdbsum/5j6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6t ProSAT]</span></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=5j6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6t OCA], [http://pdbe.org/5j6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j6t RCSB], [http://www.ebi.ac.uk/pdbsum/5j6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ALBO1_BOAAL ALBO1_BOAAL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Boana albopunctata]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Crusca, E]] | + | [[Category: Crusca Jr E]] |
| - | [[Category: Liao, L M]] | + | [[Category: Liao LM]] |
| - | [[Category: Matos, C O]] | + | [[Category: Matos CO]] |
| - | [[Category: Oliveira, A L]] | + | [[Category: Oliveira AL]] |
| - | [[Category: Antimicrobial peptide]]
| + | |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Dpc]]
| + | |
| - | [[Category: Hylin-a1 analogue]]
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| Structural highlights
Function
ALBO1_BOAAL
Publication Abstract from PubMed
Antimicrobial peptides are recognized candidates with pharmaceutical potential against epidemic emerging multi-drug resistant bacteria. In this study, we use nuclear magnetic resonance spectroscopy and molecular dynamics simulations to determine the unknown structure and evaluate the interaction with dodecylphosphatidylcholine (DPC) and sodium dodecylsulphate (SDS) micelles with three W6 -Hylin-a1 analogs antimicrobial peptides (HyAc, HyK, and HyD). The HyAc, HyK, and HyD bound to DPC micelles are all formed by a unique alpha-helix structure. Moreover, all peptides reach the DPC micelles' core, which thus suggests that the N-terminal modifications do not influence the interaction with zwiterionic surfaces. On the other hand, only HyAc and HyK peptides are able to penetrate the SDS micelle core while HyD remains always at its surface. The stability of the alpha-helical structure, after peptide-membrane interaction, can also be important to the second step of peptide insertion into the membrane hydrophobic core during permeabilization. Copyright (c) 2017 European Peptide Society and John Wiley & Sons, Ltd.
NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles.,Crusca E Jr, Camara AS, Matos CO, Marchetto R, Cilli EM, Liao LM, Lima de Oliveira A J Pept Sci. 2017 Jun;23(6):421-430. doi: 10.1002/psc.3002. Epub 2017 Apr 20. PMID:28425152[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crusca E Jr, Camara AS, Matos CO, Marchetto R, Cilli EM, Liao LM, Lima de Oliveira A. NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles. J Pept Sci. 2017 Jun;23(6):421-430. doi: 10.1002/psc.3002. Epub 2017 Apr 20. PMID:28425152 doi:http://dx.doi.org/10.1002/psc.3002
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