2m3n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Peptide leucine arginine== | |
| + | <StructureSection load='2m3n' size='340' side='right'caption='[[2m3n]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2m3n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_pipiens Lithobates pipiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3N FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2m3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3n OCA], [https://pdbe.org/2m3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3n RCSB], [https://www.ebi.ac.uk/pdbsum/2m3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PLR_LITPI PLR_LITPI] Mast cell degranulating peptide. Antiproliferative activity against human breast and ovarian tumor cell lines in vitro. Inhibits granulopoiesis in rat in vitro. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against Gram-positive bacteria B.megaterium Bm11, S.lentus and M.luteus, and antifungal activity against C.tropicalis, C.guiller-mondii and P.nicotianae spores. Has hemolytic activity. The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores.<ref>PMID:11099505</ref> <ref>PMID:14636071</ref> <ref>PMID:9673585</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The peptide leucine arginine (pLR) belongs to a new class of cyclic peptides isolated from frog skin. Its primary sequence is similar to the reactive loop of plant Bowman-Birk inhibitors (BBI), and the recently discovered circular sunflower trypsin inhibitor-1 (SFTI-1). The conformational properties of pLR in solution were determined by NMR spectroscopy and revealed excellent structural similarity to BBI and SFTI-1. Moreover, pLR is a highly potent trypsin inhibitor, with Ki values in the nanomolar range, and, due to its small size, a potential inhibitor of the serine protease tryptase. Since tryptase plays a crucial role in the development of allergic airway inflammation, the therapeutic potential of pLR in a murine asthma model was investigated. Treatment of ovalbumin-sensitized mice with pLR during allergen challenge reduced the acute asthma phenotype. Most importantly, application even at the end of a long-lasting chronic asthma model decreased the development of chronic airway inflammation and tissue remodeling. | ||
| - | + | Therapeutic Potential of the Peptide Leucine Arginine As a New Nonplant Bowman-Birk-Like Serine Protease Inhibitor.,Rothemund S, Sonnichsen FD, Polte T J Med Chem. 2013 Aug 29. PMID:23988198<ref>PMID:23988198</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2m3n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lithobates pipiens]] | ||
| + | [[Category: Polte T]] | ||
Current revision
Peptide leucine arginine
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