1qx9: Difference between revisions
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==Structure of a cyclic indolicidin peptide derivative with higher charge== | ==Structure of a cyclic indolicidin peptide derivative with higher charge== | ||
<StructureSection load='1qx9' size='340' side='right'caption='[[1qx9 | <StructureSection load='1qx9' size='340' side='right'caption='[[1qx9]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qx9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX9 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1qx9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QX9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx9 OCA], [https://pdbe.org/1qx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CTHL4_BOVIN CTHL4_BOVIN] Potent microbicidal activity; active against S.aureus and E.coli. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Friedrich | [[Category: Friedrich CL]] | ||
[[Category: Hancock | [[Category: Hancock RE]] | ||
[[Category: Powers | [[Category: Powers JP]] | ||
[[Category: Rozek | [[Category: Rozek A]] | ||
Latest revision as of 07:50, 17 October 2024
Structure of a cyclic indolicidin peptide derivative with higher chargeStructure of a cyclic indolicidin peptide derivative with higher charge
Structural highlights
FunctionCTHL4_BOVIN Potent microbicidal activity; active against S.aureus and E.coli. Publication Abstract from PubMedIndolicidin is an antimicrobial cationic peptide with broad-spectrum activity isolated from bovine neutrophils. An indolicidin analogue CP-11, ILKKWPWWPWRRK-NH(2), with improved activity against Gram-negative bacteria had increased positive charge and amphipathicity while maintaining the short length of the parent molecule. The structure of CP-11 in the presence of dodecylphosphocholine (DPC) micelles was determined using nuclear magnetic resonance spectroscopy. CP-11 was found to be an amphipathic molecule with a U-shaped backbone bringing the N- and C-termini in close proximity. On the basis of this close proximity, a cyclic disulfide-bonded peptide cycloCP-11, ICLKKWPWWPWRRCK-NH(2), was designed to stabilize the lipid-bound structure and to increase protease resistance. The three-dimensional structure of cycloCP-11 was determined under the same conditions as for the linear peptide and was found to be similar to CP-11. Both CP-11 and cycloCP-11 associated with phospholipid membranes in a similar manner as indicated by circular dichroism and fluorescence spectra. The minimal inhibitory concentrations of CP-11 and cycloCP-11 for a range of bacteria differed by no more than 2-fold, and they were nonhemolytic at concentrations up to 256 microg/mL. Cyclization was found to greatly increase protease stability. The half-life of cycloCP-11 in the presence of trypsin was increased by 4.5-fold from 4 to 18 min. More importantly, the antibacterial activity of cycloCP-11, but not that of CP-11, in the presence of trypsin was completely retained up to 90 min since the major degradation product was equally active. A structural comparison of CP-11 and cycloCP-11 revealed that the higher trypsin resistance of cycloCP-11 may be due to the more compact packing of lysine and tryptophan side chains. These findings suggest that cyclization may serve as an important strategy in the rational design of antimicrobial peptides. Structure-based design of an indolicidin peptide analogue with increased protease stability.,Rozek A, Powers JP, Friedrich CL, Hancock RE Biochemistry. 2003 Dec 9;42(48):14130-8. PMID:14640680[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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