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7ovz

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SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL

Structural highlights

7ovz 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.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

M1H1_BOMMX Maximin-1 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 does not possess a significant anti-HIV activity. It shows high spermicidal activity.^[1] Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.^[2]

Publication Abstract from PubMed

Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three-dimensional structural model was obtained in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an alpha-helical structure from residue Ile(2) to Ala(26) . The peptide is amphipathic, showing a clear separation between polar and non-polar residues. The interactions with sodium dodecyl sulfate micelles, a widely-used bacterial membrane-mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an alpha-helical conformation, occasionally displaying a flexibility around the Gly(9) and Gly(16) residues, 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 the micelle.

Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.,Timmons PB, Hewage CM J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur J Immunol. 2005 Apr;35(4):1220-9. doi: 10.1002/eji.200425615. PMID:15770703 doi:http://dx.doi.org/10.1002/eji.200425615
↑ Lee WH, Li Y, Lai R, Li S, Zhang Y, Wang W. Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur J Immunol. 2005 Apr;35(4):1220-9. doi: 10.1002/eji.200425615. PMID:15770703 doi:http://dx.doi.org/10.1002/eji.200425615
↑ Timmons PB, Hewage CM. Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1. J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121 doi:http://dx.doi.org/10.1002/psc.3370

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7ovz"

Categories: Bombina maxima | Large Structures | Hewage CM | Timmons PB

@@ Line 1: / Line 1: @@
 ==SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL==
-<StructureSection load='7ovz' size='340' side='right'caption='[[7ovz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='7ovz' size='340' side='right'caption='[[7ovz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7ovz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OVZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7ovz]] 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=7OVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OVZ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6hz2|6hz2]]</div></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=7ovz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ovz OCA], [https://pdbe.org/7ovz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ovz RCSB], [https://www.ebi.ac.uk/pdbsum/7ovz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ovz ProSAT]</span></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=7ovz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ovz OCA], [https://pdbe.org/7ovz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ovz RCSB], [https://www.ebi.ac.uk/pdbsum/7ovz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ovz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/M1H1_BOMMX M1H1_BOMMX]] Maximin-1 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 does not possess a significant anti-HIV activity. It shows high spermicidal activity.<ref>PMID:15770703</ref>   Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.<ref>PMID:15770703</ref>
+[https://www.uniprot.org/uniprot/M1H1_BOMMX M1H1_BOMMX] Maximin-1 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 does not possess a significant anti-HIV activity. It shows high spermicidal activity.<ref>PMID:15770703</ref>   Maximin-H1 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.<ref>PMID:15770703</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Bombina maxima]]
 [[Category: Large Structures]]
-[[Category: Hewage, C M]]
+[[Category: Hewage CM]]
-[[Category: Timmons, P B]]
+[[Category: Timmons PB]]
-[[Category: Antimicrobial peptide]]
-[[Category: Antimicrobial protein]]
-[[Category: Maximin 1]]

7ovz

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Current revision

SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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