2L5R
Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C
Summary for 2L5R
| Entry DOI | 10.2210/pdb2l5r/pdb |
| NMR Information | BMRB: 17281 |
| Descriptor | Antimicrobial peptide Alyteserin-1C (1 entity in total) |
| Functional Keywords | alpha helix, antimicrobial protein |
| Biological source | Alytes obstetricans (midwife toad) |
| Total number of polymer chains | 1 |
| Total formula weight | 2270.71 |
| Authors | Subasinghage, A.P.,Hewage, C.M.,Conlon, M. (deposition date: 2010-11-03, release date: 2011-11-23, Last modification date: 2024-05-01) |
| Primary citation | Subasinghage, A.P.,O'Flynn, D.,Conlon, J.M.,Hewage, C.M. Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c. Biochim.Biophys.Acta, 1808:1975-1984, 2011 Cited by PubMed Abstract: Alyteserin-1c (GLKEIFKAGLGSLVKGIAAHVAS.NH(2)), first isolated from skin secretions of the midwife toad Alytes obstetricans, shows selective growth-inhibitory activity against Gram-negative bacteria. The structures of alyteserin-1c and its more potent and less haemolytic analogue [E4K]alyteserin-1c were investigated in various solution and membrane mimicking environments by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide displays a lack of secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by an extended alpha helix between residues Leu(2) and Val(21). Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21). Positional studies of the peptides in SDS, DPC and DHPC media show that the N-terminal and central residues lie inside the micelle while C-terminal residues beyond Ala(19) do not interact with the micelles. PubMed: 21565166DOI: 10.1016/j.bbamem.2011.04.012 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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