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5wrx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==VG13P structure in LPS== | |
| + | <StructureSection load='5wrx' size='340' side='right' caption='[[5wrx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wrx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WRX 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=5wrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wrx OCA], [http://pdbe.org/5wrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wrx RCSB], [http://www.ebi.ac.uk/pdbsum/5wrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wrx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In this study, we report an interaction study of a 13-residue analogue peptide VG13P (VARGWGRKCPLFG), derived from a designed VG16KRKP peptide (VARGWKRKCPLFGKGG), with a Lys6Gly mutation and removal of the last three residues Lys14-Gly15-Gly16, in lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria and responsible for sepsis or septic shock. VG13P displays an enhanced anti-endotoxin property as evident from significant reduction in LPS-induced TNF-alpha gene expression levels in a monocytic cell line, while it retains almost unchanged antimicrobial activity as its parent VG16KRKP against Gram-negative bacterial as well as fungal pathogens. In addition, in vitro LPS binding properties of VG13P in comparison to its parent VG16KRKP also remained unhindered, suggesting that the flexible C-terminal end of VG16KRKP may not play a major role in its observed antibacterial and LPS binding properties. An NMR-resolved solution structure of VG13P in LPS reveals two consecutive beta-turns: one at the N-terminus, followed by another at the central region, closely resembling a rocking chair. The crucial Lys6Gly mutation along with C-terminal truncation from VG16KRKP reorients the hydrophobic hub in VG13P in a unique way so as to fold the N-terminal end back on itself, forming a turn and allowing Val1 and Ala2 to interact with Leu11 and Phe12 to bring the hydrophobic residues closer together to form a more compact hub compared to its parent. The hub is further strengthened via CH-pi interaction between Gly4 and Phe12. This accounts for its improved anti-endotoxin activity as well as to its uninterrupted antimicrobial activity. | ||
| - | + | Structural and Dynamic Insights into a Glycine-Mediated Short Analogue of a Designed Peptide in Lipopolysaccharide Micelles: Correlation Between Compact Structure and Anti-Endotoxin Activity.,Datta A, Jaiswal N, Ilyas H, Debnath S, Biswas K, Kumar D, Bhunia A Biochemistry. 2017 Mar 7;56(9):1348-1362. doi: 10.1021/acs.biochem.6b01229. Epub , 2017 Feb 21. PMID:28168875<ref>PMID:28168875</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5wrx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bhunia, A]] | ||
| + | [[Category: Datta, A]] | ||
| + | [[Category: Antimicrobial peptide]] | ||
| + | [[Category: Antimicrobial protein]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Endotoxin neutralisation]] | ||
| + | [[Category: Turn and loop-like structure]] | ||
Revision as of 12:54, 10 May 2017
VG13P structure in LPS
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