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| | ==Peptide leucine arginine== | | ==Peptide leucine arginine== |
| - | <StructureSection load='2m3n' size='340' side='right'caption='[[2m3n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2m3n' size='340' side='right'caption='[[2m3n]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2m3n]] is a 1 chain structure. 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> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jbl|1jbl]], [[1gm2|1gm2]]</div></td></tr> | + | </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> | | <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> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PLR_RANPI PLR_RANPI]] 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:9673585</ref> <ref>PMID:14636071</ref>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Polte, T]] | + | [[Category: Lithobates pipiens]] |
| - | [[Category: Bowman birk inhibitor]] | + | [[Category: Polte T]] |
| - | [[Category: Hydrolase inhibitor]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Salmon AL, Cross LJ, Irvine AE, Lappin TR, Dathe M, Krause G, Canning P, Thim L, Beyermann M, Rothemund S, Bienert M, Shaw C. Peptide leucine arginine, a potent immunomodulatory peptide isolated and structurally characterized from the skin of the Northern Leopard frog, Rana pipiens. J Biol Chem. 2001 Mar 30;276(13):10145-52. Epub 2000 Nov 30. PMID:11099505 doi:10.1074/jbc.M009680200
- ↑ Mangoni ML, Papo N, Mignogna G, Andreu D, Shai Y, Barra D, Simmaco M. Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity. Biochemistry. 2003 Dec 2;42(47):14023-35. PMID:14636071 doi:10.1021/bi034521l
- ↑ . Joint British Association and Irish Association Cancer Research Meeting. Dublin, Ireland, 21-24 June 1998. Abstracts. Br J Cancer. 1998;78 Suppl 1:1-78. PMID:9673585
- ↑ Rothemund S, Sonnichsen FD, Polte T. Therapeutic Potential of the Peptide Leucine Arginine As a New Nonplant Bowman-Birk-Like Serine Protease Inhibitor. J Med Chem. 2013 Aug 29. PMID:23988198 doi:10.1021/jm4005362
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