6g4u

The solution NMR structure of brevinin-1BYa in dodecylphosphocholine micelles

spinqualitylabelsall models 6g4u Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6g4u is a 1 chain structure with sequence from Rana boylii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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