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6hz2
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6hz2 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL== | |
| + | <StructureSection load='6hz2' size='340' side='right'caption='[[6hz2]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hz2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombina_maxima Bombina maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HZ2 FirstGlance]. <br> | ||
| + | </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=6hz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hz2 OCA], [https://pdbe.org/6hz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hz2 RCSB], [https://www.ebi.ac.uk/pdbsum/6hz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hz2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/M3112_BOMMX 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.<ref>PMID:11835991</ref> Maximin-H11 shows antimicrobial activity against bacteria and against the fungus C.albicans. Shows strong hemolytic activity (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:30734844</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6hz2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bombina maxima]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Benetti S]] | ||
| + | [[Category: Hewage CM]] | ||
| + | [[Category: Timmons PB]] | ||
Current revision
SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL
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