6twg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 6twg is ON HOLD Authors: Cantini, F., Bouchemal, N., Savarin, P., Sette, M. Description: Solution structure of antimicrobial peptide, crabrolin Plu...)
Current revision (06:09, 19 June 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6twg is ON HOLD
+
==Solution structure of antimicrobial peptide, crabrolin Plus in the presence of Lipopolysaccharide==
 +
<StructureSection load='6twg' size='340' side='right'caption='[[6twg]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TWG FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6twg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6twg OCA], [https://pdbe.org/6twg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6twg RCSB], [https://www.ebi.ac.uk/pdbsum/6twg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6twg ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Antimicrobial peptides (AMPs) appear as chemical compounds of increasing interest for their role in killing bacteria and, more recently, for their ability to bind endotoxin (lipopolysaccharide, LPS) that is released during bacterial infection and that may lead to septic shock. This dual role in the mechanism of action can further be enhanced in a synergistic way when two or more AMPs are combined together. Not all AMPs are able to bind LPS, suggesting that several modes of binding to the bacterial surface may exist. Here we analyze a natural AMP, crabrolin, and two mutated forms, one with increased positive charge (Crabrolin Plus) and the other with null charge (Crabrolin Minus), and compare their binding abilities to LPS. While Crabrolin WT as well Crabrolin Minus do not show binding to LPS, the mutated Crabrolin Plus exhibits binding and forms a well defined structure in the presence of LPS. The results strengthen the importance of positive charges for the binding to LPS and suggest the mutated form with increased positive charge as a promising candidate for antimicrobial and antiseptic activity.
-
Authors: Cantini, F., Bouchemal, N., Savarin, P., Sette, M.
+
Effect of positive charges in the structural interaction of crabrolin isoforms with lipopolysaccharide.,Cantini F, Luzi C, Bouchemal N, Savarin P, Bozzi A, Sette M J Pept Sci. 2020 Jun 25:e3271. doi: 10.1002/psc.3271. PMID:32585759<ref>PMID:32585759</ref>
-
Description: Solution structure of antimicrobial peptide, crabrolin Plus in the presence of Lipopolysaccharide
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Cantini, F]]
+
<div class="pdbe-citations 6twg" style="background-color:#fffaf0;"></div>
-
[[Category: Bouchemal, N]]
+
== References ==
-
[[Category: Sette, M]]
+
<references/>
-
[[Category: Savarin, P]]
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Bouchemal N]]
 +
[[Category: Cantini F]]
 +
[[Category: Savarin P]]
 +
[[Category: Sette M]]

Current revision

Solution structure of antimicrobial peptide, crabrolin Plus in the presence of Lipopolysaccharide

PDB ID 6twg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools