6hz2 | pdb_00006hz2

SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL

spinqualitylabelsall models 6hz2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hz2 is a 1 chain structure with sequence from Bombina maxima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M3112_BOMMX Maximin-3 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It possess a significant anti-HIV activity. It shows high spermicidal activity. Maximin-H11 shows antimicrobial activity against bacteria and against the fungus C.albicans. Shows strong hemolytic activity (By similarity). Publication Abstract from PubMed Maximin 3 is a 27-residue-long cationic antimicrobial peptide found in the skin secretion and brain of the Chinese red-belly toad Bombina maxima. The peptide is of biological interest as it possesses anti-HIV activity, not found in the other maximin peptides, in addition to antimicrobial, antitumor and spermicidal activities. The three-dimensional structure of maximin 3 was obtained in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture using two-dimensional NMR spectroscopy. Maximin 3 was found to adopt an alpha-helical structure from residue G1 to A22, and a coil structure with a helical propensity in the C-terminal tail. The peptide is amphipathic, showing a clear separation between polar and hydrophobic residues. Interactions with sodium dodecyl sulfate micelles, a widely used bacterial membrane-mimicking environment, were modeled using molecular dynamics simulations. The peptide maintained an alpha-helical conformation, occasionally displaying a flexibility around residues G9 and G16, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with it. NMR model structure of the antimicrobial peptide maximin 3.,Benetti S, Timmons PB, Hewage CM Eur Biophys J. 2019 Feb 8. pii: 10.1007/s00249-019-01346-7. doi:, 10.1007/s00249-019-01346-7. PMID:30734844 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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