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2MN8

NMR structure of a peptoid analogue of maculatin G15 containing cis-Nleu at position 13

Summary for 2MN8
Entry DOI10.2210/pdb2mn8/pdb
Related2MMJ 2MN9
NMR InformationBMRB: 19882
Descriptormaculatin G15 (1 entity in total)
Functional Keywordspeptoid, n-substituted glycine, maculatin, antimicrobial peptide, antimicrobial protein
Biological sourceLitoria genimaculata (Green-eyed tree frog)
Total number of polymer chains1
Total formula weight2121.53
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 citationUggerhj, 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: 25063337
DOI: 10.1016/j.febslet.2014.07.016
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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