2ox2
From Proteopedia
(Difference between revisions)
m (Protected "2ox2" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[ | + | ==Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles== |
| + | <StructureSection load='2ox2' size='340' side='right' caption='[[2ox2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ox2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OX2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OX2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qvk|1qvk]], [[1qvl|1qvl]], [[1ski|1ski]], [[1skl|1skl]], [[1skk|1skk]], [[2otq|2otq]]</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=2ox2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ox2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ox2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ox2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd. | ||
| - | + | Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity.,Appelt C, Wessolowski A, Dathe M, Schmieder P J Pept Sci. 2007 Nov 6;. PMID:17985394<ref>PMID:17985394</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Appelt, C.]] | [[Category: Appelt, C.]] | ||
[[Category: Dathe, M.]] | [[Category: Dathe, M.]] | ||
Revision as of 11:23, 20 October 2014
Structure of the cantionic, antimicrobial hexapeptide cyclo(RRWWFR) bound to DPC-micelles
| |||||||||||
