2MN8
NMR structure of a peptoid analogue of maculatin G15 containing cis-Nleu at position 13
Summary for 2MN8
| Entry DOI | 10.2210/pdb2mn8/pdb |
| Related | 2MMJ 2MN9 |
| NMR Information | BMRB: 19882 |
| Descriptor | maculatin G15 (1 entity in total) |
| Functional Keywords | peptoid, n-substituted glycine, maculatin, antimicrobial peptide, antimicrobial protein |
| Biological source | Litoria genimaculata (Green-eyed tree frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 2121.53 |
| Authors | Uggerhoej, L.E.,Guentert, P.,Wimmer, R. (deposition date: 2014-03-29, release date: 2014-07-23, Last modification date: 2014-12-03) |
| Primary citation | Uggerhj, L.E.,Munk, J.K.,Hansen, P.R.,Guntert, P.,Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces. Febs Lett., 588:3291-3297, 2014 Cited by PubMed Abstract: The inclusion of peptoid monomers into antimicrobial peptides (AMPs) increases their proteolytic resistance, but introduces conformational flexibility (reduced hydrogen bonding ability and cis/trans isomerism). We here use NMR spectroscopy to answer how the insertion of a peptoid monomer influences the structure of a regular α-helical AMP upon interaction with a dodecyl phosphocholine (DPC) micelle. Insertion of [(2-methylpropyl)amino]acetic acid in maculatin-G15 shows that the structural change and conformational flexibility depends on the site of insertion. This is governed by the micelle interaction of the amphipathic helices flanking the peptoid monomer and the side chain properties of the peptoid and its preceding residue. PubMed: 25063337DOI: 10.1016/j.febslet.2014.07.016 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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