1hu6: Difference between revisions
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New page: left|200px<br /><applet load="1hu6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hu6" /> '''SOLUTION STRUCTURE OF G10 NOVISPIRIN'''<br /... |
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== | ==SOLUTION STRUCTURE OF G10 NOVISPIRIN== | ||
We studied three model antibacterial peptides that resembled the | <StructureSection load='1hu6' size='340' side='right'caption='[[1hu6]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hu6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HU6 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=1hu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hu6 OCA], [https://pdbe.org/1hu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hu6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hu6 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We studied three model antibacterial peptides that resembled the N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to human epithelial cells and hemolytic for human erythrocytes. Single residue substitutions to ovispirin-1 yielded two substantially less cytotoxic peptides (novispirins), with intact antimicrobial properties. One of these, novispirin G-10, differed from ovispirin-1 only by containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7. We determined the three-dimensional solution structures of all three peptides by circular dichroism spectroscopy and two-dimensional nuclear magnetic resonance spectroscopy. Although all retained an amphipathic helical structure in 2,2,2-trifluoroethanol, they manifested subtle fine-structural changes that evidently impacted their activities greatly. These findings show that simple structural modifications can 'fine-tune' an antimicrobial peptide to minimize unwanted cytotoxicity while retaining its desired activity. | |||
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides.,Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF Protein Eng. 2002 Mar;15(3):225-32. PMID:11932493<ref>PMID:11932493</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1hu6" style="background-color:#fffaf0;"></div> | ||
[[Category: Forsyth | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Sawai | [[Category: Large Structures]] | ||
[[Category: Tack | [[Category: Forsyth WR]] | ||
[[Category: Waring | [[Category: Kearney WR]] | ||
[[Category: Lehrer RI]] | |||
[[Category: McCray Jr PB]] | |||
[[Category: Sawai MV]] | |||
[[Category: Tack BF]] | |||
[[Category: Waring AJ]] | |||
Latest revision as of 18:39, 29 November 2023
SOLUTION STRUCTURE OF G10 NOVISPIRIN
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