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| - | {{Seed}} | |
| - | [[Image:1zrx.png|left|200px]] | |
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| - | <!-- | + | ==solution structure of stomoxyn in H20/TFE 50%== |
| - | The line below this paragraph, containing "STRUCTURE_1zrx", creates the "Structure Box" on the page.
| + | <StructureSection load='1zrx' size='340' side='right'caption='[[1zrx]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1zrx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stomoxys_calcitrans Stomoxys calcitrans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRX FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrx OCA], [https://pdbe.org/1zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zrx RCSB], [https://www.ebi.ac.uk/pdbsum/1zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zrx ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1zrx| PDB=1zrx | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/STMX_STOCA STMX_STOCA] Has antimicrobial activity against most Gram-positive and Gram-negative bacteria, filamentous fungi and yeasts tested. Has trypanolytic effect on T.b.rhodesiense and limited hemolytic activity against bovine red blood cells.<ref>PMID:12372834</ref> May play an important role in protecting the stored blood in the anterior midgut from microorganisms prior to digestion. Adopts an amphipathic alpha-helical structure only in the presence of an organic solvent that mimics a phospholipid membrane.<ref>PMID:12372834</ref> <ref>PMID:12372834</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Stomoxyn and spinigerin belong to the class of linear cysteine-free insect antimicrobial peptides that kill a range of microorganisms, parasites, and some viruses but without any lytic activity against mammalian erythrocytes. Stomoxyn is localized in the gut epithelium of the nonvector stable fly that is sympatric with the trypanosome vector tsetse fly. Spinigerin is stored and secreted by hemocytes from the fungus-growing termite. The structure of synthetic stomoxyn and spinigerin in aqueous solution and in TFE/water mixtures was analyzed by CD and NMR spectroscopy combined with molecular modeling calculations. Stomoxyn and spinigerin adopt a flexible random coil structure in water while both assume a stable helical structure in the presence of TFE. In 50% TFE, the structure of stomoxyn is typical of cecropins, including an amphipathic helix at the N-terminus and a hydrophobic C-terminus with helical features that probably fold in a helical conformation at higher TFE concentration. In contrast to stomoxyn, spinigerin acquires very rapidly a helical conformation. In 10% TFE the helix is highly bent and the structure is poorly defined. In 50% TFE, the helical structure is well defined all along its sequence, and the slightly bent alpha-helix displays an amphiphilic character, as observed for magainin 2. The structural similarities between stomoxyn and cecropin A from Hyalophora cecropia and between spinigerin and magainin 2 suggest a similar mode of action on the bacterial membranes of both pairs of peptides. Our results also confirm that TFE induces helix formation and propagation for amino acids showing helical propensity in water but also enhances the helix propagation propensity of nonpolar beta-branched residues. |
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| - | ===solution structure of stomoxyn in H20/TFE 50%===
| + | Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.,Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F Biopolymers. 2006 Feb 5;81(2):92-103. PMID:16170803<ref>PMID:16170803</ref> |
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| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_16170803}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 1zrx" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 16170803 is the PubMed ID number.
| + | == References == |
| - | --> | + | <references/> |
| - | {{ABSTRACT_PUBMED_16170803}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | 1ZRX is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRX OCA].
| + | [[Category: Stomoxys calcitrans]] |
| - | | + | [[Category: Boulanger N]] |
| - | ==Reference==
| + | [[Category: Bulet P]] |
| - | Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation., Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F, Biopolymers. 2006 Feb 5;81(2):92-103. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16170803 16170803]
| + | [[Category: Landon C]] |
| - | [[Category: Single protein]] | + | [[Category: Meudal H]] |
| - | [[Category: Boulanger, N.]] | + | [[Category: Vovelle F]] |
| - | [[Category: Bulet, P.]] | + | |
| - | [[Category: Landon, C.]] | + | |
| - | [[Category: Meudal, H.]] | + | |
| - | [[Category: Vovelle, F.]] | + | |
| - | [[Category: Helical peptide in tfe]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:06:48 2008''
| + | |
| Structural highlights
Function
STMX_STOCA Has antimicrobial activity against most Gram-positive and Gram-negative bacteria, filamentous fungi and yeasts tested. Has trypanolytic effect on T.b.rhodesiense and limited hemolytic activity against bovine red blood cells.[1] May play an important role in protecting the stored blood in the anterior midgut from microorganisms prior to digestion. Adopts an amphipathic alpha-helical structure only in the presence of an organic solvent that mimics a phospholipid membrane.[2] [3]
Publication Abstract from PubMed
Stomoxyn and spinigerin belong to the class of linear cysteine-free insect antimicrobial peptides that kill a range of microorganisms, parasites, and some viruses but without any lytic activity against mammalian erythrocytes. Stomoxyn is localized in the gut epithelium of the nonvector stable fly that is sympatric with the trypanosome vector tsetse fly. Spinigerin is stored and secreted by hemocytes from the fungus-growing termite. The structure of synthetic stomoxyn and spinigerin in aqueous solution and in TFE/water mixtures was analyzed by CD and NMR spectroscopy combined with molecular modeling calculations. Stomoxyn and spinigerin adopt a flexible random coil structure in water while both assume a stable helical structure in the presence of TFE. In 50% TFE, the structure of stomoxyn is typical of cecropins, including an amphipathic helix at the N-terminus and a hydrophobic C-terminus with helical features that probably fold in a helical conformation at higher TFE concentration. In contrast to stomoxyn, spinigerin acquires very rapidly a helical conformation. In 10% TFE the helix is highly bent and the structure is poorly defined. In 50% TFE, the helical structure is well defined all along its sequence, and the slightly bent alpha-helix displays an amphiphilic character, as observed for magainin 2. The structural similarities between stomoxyn and cecropin A from Hyalophora cecropia and between spinigerin and magainin 2 suggest a similar mode of action on the bacterial membranes of both pairs of peptides. Our results also confirm that TFE induces helix formation and propagation for amino acids showing helical propensity in water but also enhances the helix propagation propensity of nonpolar beta-branched residues.
Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.,Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F Biopolymers. 2006 Feb 5;81(2):92-103. PMID:16170803[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boulanger N, Munks RJ, Hamilton JV, Vovelle F, Brun R, Lehane MJ, Bulet P. Epithelial innate immunity. A novel antimicrobial peptide with antiparasitic activity in the blood-sucking insect Stomoxys calcitrans. J Biol Chem. 2002 Dec 20;277(51):49921-6. Epub 2002 Oct 7. PMID:12372834 doi:http://dx.doi.org/10.1074/jbc.M206296200
- ↑ Boulanger N, Munks RJ, Hamilton JV, Vovelle F, Brun R, Lehane MJ, Bulet P. Epithelial innate immunity. A novel antimicrobial peptide with antiparasitic activity in the blood-sucking insect Stomoxys calcitrans. J Biol Chem. 2002 Dec 20;277(51):49921-6. Epub 2002 Oct 7. PMID:12372834 doi:http://dx.doi.org/10.1074/jbc.M206296200
- ↑ Boulanger N, Munks RJ, Hamilton JV, Vovelle F, Brun R, Lehane MJ, Bulet P. Epithelial innate immunity. A novel antimicrobial peptide with antiparasitic activity in the blood-sucking insect Stomoxys calcitrans. J Biol Chem. 2002 Dec 20;277(51):49921-6. Epub 2002 Oct 7. PMID:12372834 doi:http://dx.doi.org/10.1074/jbc.M206296200
- ↑ Landon C, Meudal H, Boulanger N, Bulet P, Vovelle F. Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation. Biopolymers. 2006 Feb 5;81(2):92-103. PMID:16170803 doi:10.1002/bip.20370
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