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| | ==The solution NMR structure of brevinin-1BYa in 33% trifluoroethanol== | | ==The solution NMR structure of brevinin-1BYa in 33% trifluoroethanol== |
| - | <StructureSection load='6g4i' size='340' side='right'caption='[[6g4i]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6g4i' size='340' side='right'caption='[[6g4i]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6g4i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G4I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g4i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rana_boylii Rana boylii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G4I 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=6g4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g4i OCA], [http://pdbe.org/6g4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g4i RCSB], [http://www.ebi.ac.uk/pdbsum/6g4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g4i ProSAT]</span></td></tr> | + | </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=6g4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g4i OCA], [https://pdbe.org/6g4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g4i RCSB], [https://www.ebi.ac.uk/pdbsum/6g4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g4i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BR1A_RANBO BR1A_RANBO] |
| | <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: Conlon, J M]] | + | [[Category: Rana boylii]] |
| - | [[Category: Flynn, D P.O]] | + | [[Category: Conlon JM]] |
| - | [[Category: Hewage, C M]] | + | [[Category: Hewage CM]] |
| - | [[Category: Timmons, P B]] | + | [[Category: O'Flynn DP]] |
| - | [[Category: Antimicrobial peptide]] | + | [[Category: Timmons PB]] |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Cationic]]
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| - | [[Category: Rana-box]]
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| Structural highlights
Function
BR1A_RANBO
Publication Abstract from PubMed
Brevinin-1BYa (FLPILASLAAKFGPKLFCLVTKKC), first isolated from skin secretions of the foothill yellow-legged frog Rana boylii, shows broad-spectrum activity, being particularly effective against opportunistic yeast pathogens. The structure of brevinin-1BYa was investigated in various solution and membrane-mimicking environments by proton nuclear magnetic resonance ((1) H-NMR) spectroscopy and molecular modelling. The peptide does not possess a secondary structure in aqueous solution. In a 33% 2,2,2-trifluoroethanol (TFE-d3 )-H2 O solvent mixture, as well as in membrane-mimicking sodium dodecyl sulfate and dodecylphosphocholine micelles, the peptide's structure is characterised by a flexible helix-hinge-helix motif, with the hinge located at the Gly(13) /Pro(14) residues, and the two alpha-helices extending from Pro(3) to Phe(12) and from Pro(14) to Thr(21) . Positional studies involving the peptide in sodium dodecyl sulfate and dodecylphosphocholine micelles using 5-doxyl-labelled stearic acid and manganese chloride paramagnetic probes show that the peptide's helical segments lie parallel to the micellar surface, with the residues on the hydrophobic face of the amphipathic helices facing towards the micelle core and the hydrophilic residues pointing outwards, suggesting that the peptide exerts its biological activity by a non-pore-forming mechanism.
Structural and positional studies of the antimicrobial peptide brevinin-1BYa in membrane-mimetic environments.,Timmons PB, O'Flynn D, Conlon JM, Hewage CM J Pept Sci. 2019 Nov;25(11):e3208. doi: 10.1002/psc.3208. PMID:31721374[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Timmons PB, O'Flynn D, Conlon JM, Hewage CM. Structural and positional studies of the antimicrobial peptide brevinin-1BYa in membrane-mimetic environments. J Pept Sci. 2019 Nov;25(11):e3208. doi: 10.1002/psc.3208. PMID:31721374 doi:http://dx.doi.org/10.1002/psc.3208
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