2nc7: Difference between revisions
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==Antimicrobial peptide protegrin PG-5== | ==Antimicrobial peptide protegrin PG-5== | ||
<StructureSection load='2nc7' size='340' side='right'caption='[[2nc7 | <StructureSection load='2nc7' size='340' side='right'caption='[[2nc7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nc7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NC7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2nc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NC7 FirstGlance]. <br> | ||
</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=2nc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc7 OCA], [https://pdbe.org/2nc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nc7 RCSB], [https://www.ebi.ac.uk/pdbsum/2nc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc7 ProSAT]</span></td></tr> | </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=2nc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc7 OCA], [https://pdbe.org/2nc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nc7 RCSB], [https://www.ebi.ac.uk/pdbsum/2nc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PG5_PIG PG5_PIG] Microbicidal activity. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sus scrofa]] | ||
[[Category: | [[Category: Aganov AV]] | ||
[[Category: | [[Category: Klochkov VV]] | ||
[[Category: | [[Category: Klochkova EA]] | ||
[[Category: | [[Category: Kolosova OA]] | ||
Revision as of 13:00, 14 June 2023
Antimicrobial peptide protegrin PG-5Antimicrobial peptide protegrin PG-5
Structural highlights
FunctionPG5_PIG Microbicidal activity. Publication Abstract from PubMedProtegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong dalphaalpha NOE effects between residues R18 and F12, V14, and V16. These "inconsistent" with monomer structure NOEs appears due to formation of an additional antiparallel beta-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric beta-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data. Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.,Usachev KS, Kolosova OA, Klochkova EA, Yulmetov AR, Aganov AV, Klochkov VV Eur Biophys J. 2017 Apr;46(3):293-300. doi: 10.1007/s00249-016-1167-5. Epub 2016 , Sep 2. PMID:27589857[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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