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| | ==Solution structure of the synthetic mytilin== | | ==Solution structure of the synthetic mytilin== |
| - | <StructureSection load='2eem' size='340' side='right'caption='[[2eem]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2eem' size='340' side='right'caption='[[2eem]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2eem]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EEM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2eem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EEM FirstGlance]. <br> |
| - | </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=2eem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eem OCA], [http://pdbe.org/2eem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eem RCSB], [http://www.ebi.ac.uk/pdbsum/2eem PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eem ProSAT]</span></td></tr> | + | </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=2eem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eem OCA], [https://pdbe.org/2eem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eem RCSB], [https://www.ebi.ac.uk/pdbsum/2eem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eem ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYTB_MYTED MYTB_MYTED]] Has antibacterial and antiviral activity. | + | [https://www.uniprot.org/uniprot/MYTB_MYTED MYTB_MYTED] Has antibacterial and antiviral activity. |
| | <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: Aumelas, A]] | + | [[Category: Mytilus edulis]] |
| - | [[Category: Roch, P]] | + | [[Category: Aumelas A]] |
| - | [[Category: Yang, Y]] | + | [[Category: Roch P]] |
| - | [[Category: Antibiotic]] | + | [[Category: Yang Y]] |
| - | [[Category: Antiviral peptide]]
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| - | [[Category: Cystein stabilized alpha-beta motif]]
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| - | [[Category: Disulfide bond]]
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| - | [[Category: Mussel]]
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| Structural highlights
Function
MYTB_MYTED Has antibacterial and antiviral activity.
Publication Abstract from PubMed
Mytilin is a 34-residue antibacterial peptide from the mussel Mytilus galloprovincialis, which in addition possesses in vitro antiviral activity. The three-dimensional solution structure of the synthetic mytilin was established by using 1H NMR and consists of the common cysteine-stabilized alphabeta motif close to the one observed in the mussel defensin MGD-1. Mytilin is characterized by 8 cysteines engaged in four disulfide bonds (2-27, 6-29, 10-31, and 15-34) only involving the beta-strand II. Hydrophilic and hydrophobic areas of mytilin account for 63% and 37%, respectively, a ratio very close to that of MGD-1 (64% and 36%). One linear and three cyclic fragments were designed from the interstrand loop sequence known to retain the biological activities in MGD-1. Only the fragment of 10 amino acids (C10C) constrained by two disulfide bonds in a stable beta-hairpin structure was able to inhibit the mortality of Palaemon serratus shrimp injected with white spot syndrome virus (WSSV). Fifty percent inhibition was obtained by in vitro pre-incubation of WSSV with 45muM of C10C compared with 7muM for mytilin. Interaction between the fragment and the virus occurred very rapidly as 40% survival was recorded after only 1min of pre-incubation. In addition, C10C was capable of inhibiting in vitro growth of Vibrio splendidus LGP32 (MIC 125muM), Vibrio anguillarum (MIC 2mM), Micrococcus lysodeikticus and Escherichia coli (MIC 1mM). Destroying the cysteine-stabilized alphabeta structure or shortening the C1OC fragment to the C6C fragment with only one disulfide bond resulted in loss of both antiviral and antibacterial activities. Increasing the positive net charge did not enforce the antibacterial activity and completely suppressed the antiviral one. The C10C-designed peptide from mytilin appeared comparable in composition and structure with protegrin, tachyplesin and polyphemusin.
NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides.,Roch P, Yang Y, Toubiana M, Aumelas A Dev Comp Immunol. 2008;32(3):227-38. Epub 2007 Jun 26. PMID:17628674[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roch P, Yang Y, Toubiana M, Aumelas A. NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides. Dev Comp Immunol. 2008;32(3):227-38. Epub 2007 Jun 26. PMID:17628674 doi:http://dx.doi.org/S0145-305X(07)00083-3
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