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6hz2

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SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL

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.
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.^[1] 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^[2]

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

References

↑ Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Peptides. 2002 Mar;23(3):427-35. PMID:11835991
↑ Benetti S, Timmons PB, Hewage CM. NMR model structure of the antimicrobial peptide maximin 3. Eur Biophys J. 2019 Feb 8. pii: 10.1007/s00249-019-01346-7. doi:, 10.1007/s00249-019-01346-7. PMID:30734844 doi:http://dx.doi.org/10.1007/s00249-019-01346-7

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/6hz2"

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

@@ Line 1: / Line 1: @@
 ==SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL==
-<StructureSection load='6hz2' size='340' side='right'caption='[[6hz2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6hz2' size='340' side='right'caption='[[6hz2]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6hz2]] is a 1 chain structure. 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>
+<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).
+[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 ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Bombina maxima]]
 [[Category: Large Structures]]
-[[Category: Benetti, S]]
+[[Category: Benetti S]]
-[[Category: Hewage, C M]]
+[[Category: Hewage CM]]
-[[Category: Timmons, P B]]
+[[Category: Timmons PB]]
-[[Category: Antimicrobial protein]]
-[[Category: Maximin 3 antimicrobial peptide alpha helix]]

6hz2

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Current revision

SOLUTION NMR STRUCTURE OF MAXIMIN 3 IN 50% TRIFLUOROETHANOL

Structural highlights

Function

Publication Abstract from PubMed

References

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