2nc7: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:


==Antimicrobial peptide protegrin PG-5==
==Antimicrobial peptide protegrin PG-5==
<StructureSection load='2nc7' size='340' side='right' caption='[[2nc7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2nc7' size='340' side='right'caption='[[2nc7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NC7 FirstGlance]. <br>
<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 [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc7 OCA], [http://pdbe.org/2nc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nc7 RCSB], [http://www.ebi.ac.uk/pdbsum/2nc7 PDBsum], [http://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'>[http://proteopedia.org/fgij/fg.htm?mol=2nc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc7 OCA], [http://pdbe.org/2nc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nc7 RCSB], [http://www.ebi.ac.uk/pdbsum/2nc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 17: Line 17:
</div>
</div>
<div class="pdbe-citations 2nc7" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2nc7" style="background-color:#fffaf0;"></div>
==See Also==
*[[Protegrin|Protegrin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Aganov, A V]]
[[Category: Aganov, A V]]
[[Category: Klochkov, V V]]
[[Category: Klochkov, V V]]

Revision as of 10:56, 4 November 2020

Antimicrobial peptide protegrin PG-5Antimicrobial peptide protegrin PG-5

Structural highlights

2nc7 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PG5_PIG] Microbicidal activity.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Usachev KS, Kolosova OA, Klochkova EA, Yulmetov AR, Aganov AV, Klochkov VV. Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy. Eur Biophys J. 2017 Apr;46(3):293-300. doi: 10.1007/s00249-016-1167-5. Epub 2016 , Sep 2. PMID:27589857 doi:http://dx.doi.org/10.1007/s00249-016-1167-5
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA