5M9U
Spatial structure of antimicrobial peptide arenicin-1 mutant V8R
Summary for 5M9U
| Entry DOI | 10.2210/pdb5m9u/pdb |
| NMR Information | BMRB: 34059 |
| Descriptor | Arenicin-1 (1 entity in total) |
| Functional Keywords | structure from cyana 3.97, antimicrobial protein |
| Biological source | Arenicola marina (Lugworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 2824.41 |
| Authors | Myshkin, M.Y.,Shenkarev, Z.O.,Panteleev, P.V.,Ovchinnikova, T.V. (deposition date: 2016-11-02, release date: 2017-07-26, Last modification date: 2023-06-14) |
| Primary citation | Panteleev, P.V.,Myshkin, M.Y.,Shenkarev, Z.O.,Ovchinnikova, T.V. Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity. Biochem. Biophys. Res. Commun., 482:1320-1326, 2017 Cited by PubMed Abstract: The β-hairpin antimicrobial peptides arenicins from marine polychaeta Arenicola marina exhibit a broad spectrum of antimicrobial activity and high cytotoxicity. In this study the biological activities of arenicin-1 and its therapeutically valuable analog Ar-1[V8R] were investigated. The peptide Ar-1[V8R] displays significantly reduced cytotoxicity against mammalian cells relative to the wild-type arenicin-1. At the same time, both peptides exhibit similar antibacterial activities and kinetics of bacterial membrane permeabilization. Comparative NMR analysis of the peptides spatial structures in water and membrane-mimicking environment showed that Ar-1[V8R] in contrast to arenicin has significantly lower dimerization propensity. Thus, dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity. PubMed: 27940358DOI: 10.1016/j.bbrc.2016.12.035 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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