View source for 2nc7


==Antimicrobial peptide protegrin PG-5==
<StructureSection load='2nc7' size='340' side='right'caption='[[2nc7]]' scene=''>
== Structural highlights ==
<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='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=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>
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== Publication Abstract from PubMed ==
Protegrin 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<ref>PMID:27589857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Protegrin|Protegrin]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Aganov AV]]
[[Category: Klochkov VV]]
[[Category: Klochkova EA]]
[[Category: Kolosova OA]]