1qx9

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{{Seed}}
 
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[[Image:1qx9.png|left|200px]]
 
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==Structure of a cyclic indolicidin peptide derivative with higher charge==
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The line below this paragraph, containing "STRUCTURE_1qx9", creates the "Structure Box" on the page.
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<StructureSection load='1qx9' size='340' side='right'caption='[[1qx9]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</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>
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<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>
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{{STRUCTURE_1qx9| PDB=1qx9 | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTHL4_BOVIN CTHL4_BOVIN] Potent microbicidal activity; active against S.aureus and E.coli.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Indolicidin 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.
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===Structure of a cyclic indolicidin peptide derivative with higher charge===
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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<ref>PMID:14640680</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14640680}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qx9" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14640680 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14640680}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Bos taurus]]
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1QX9 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX9 OCA].
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[[Category: Large Structures]]
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[[Category: Friedrich CL]]
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==Reference==
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[[Category: Hancock RE]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14640680 14640680]
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[[Category: Powers JP]]
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[[Category: Single protein]]
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[[Category: Rozek A]]
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[[Category: Friedrich, C L.]]
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[[Category: Hancock, R E.]]
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[[Category: Powers, J P.]]
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[[Category: Rozek, A.]]
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[[Category: Beta turn]]
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[[Category: Cyclic cationic antimicrobial peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:27:22 2008''
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Current revision

Structure of a cyclic indolicidin peptide derivative with higher charge

PDB ID 1qx9

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