2K10
Confirmational analysis of the broad-spectrum antibacterial peptide, rantuerin-2csa: identification of a full length helix-turn-helix motif
Summary for 2K10
| Entry DOI | 10.2210/pdb2k10/pdb |
| NMR Information | BMRB: 15665 |
| Descriptor | ranatuerin-2csa (1 entity in total) |
| Functional Keywords | molecular modelling, helix-turn-helix, disulfide bond, antimicrobial peptide, antimicrobial protein |
| Biological source | Rana cascadae (frogs & toads) |
| Total number of polymer chains | 1 |
| Total formula weight | 3255.98 |
| Authors | Hewage, C.M.,Subasinghage, A.P.,Conlon, M. (deposition date: 2008-02-19, release date: 2008-04-15, Last modification date: 2024-10-30) |
| Primary citation | Subasinghage, A.P.,Conlon, J.M.,Hewage, C.M. Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif. Biochim.Biophys.Acta, 1784:924-929, 2008 Cited by PubMed Abstract: Design of clinically valuable antibacterial agents based upon naturally occurring peptides requires the use of spectroscopic methods, particularly NMR, to determine the three-dimensional structure of the native peptide so that analogues with improved therapeutic properties can be made. Ranatuerin-2CSa (GILSSFKGVAKGVAKDLAG KLLETLKCKITGC), first isolated from skin secretions of the Cascades frog, Rana cascadae, represents a promising candidate for drug development. The peptide shows potent growth inhibitory activity against Escherichia coli (MIC=5 microM) and Staphylococcus aureus (MIC=10 microM) but displays haemolytic activity against human erythrocytes (LC(50)=160 microM). The solution structure of ranatuerin-2CSa was investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide lacks secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by a full length helix-turn-helix conformation between residues I(2)-L(21), L(22)-L(25) and K(26)-T(30) respectively. This structural information will facilitate the design of novel therapeutic agents based upon the ranatuerin-2CSa structure with improved antimicrobial potencies but decreased cytolytic activities against mammalian cells. PubMed: 18387372DOI: 10.1016/j.bbapap.2008.02.019 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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