2g9l
From Proteopedia
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| - | [[Image:2g9l.jpg|left|200px]] | ||
| - | + | ==The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction== | |
| - | + | <StructureSection load='2g9l' size='340' side='right'caption='[[2g9l]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2g9l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glandirana_rugosa Glandirana rugosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G9L FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=2g9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g9l OCA], [https://pdbe.org/2g9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g9l RCSB], [https://www.ebi.ac.uk/pdbsum/2g9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g9l ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | ''' | + | [https://www.uniprot.org/uniprot/GGN4_GLARU GGN4_GLARU] Has a non-hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4. | We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4. | ||
| - | + | Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.,Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:17141187<ref>PMID:17141187</ref> | |
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| - | Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4., Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2g9l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glandirana rugosa]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chi S-W]] | ||
| + | [[Category: Han K-H]] | ||
Current revision
The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction
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