6hz2: Difference between revisions
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The | ==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='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=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]] | |||
