2MMJ

Structure of a peptoid analogue of maculatin G15 in DPC micelles

2MMJ の概要

• エントリーDOI: 10.2210/pdb2mmj/pdb
• NMR情報: BMRB: 19856
• 分子名称: maculatin G15 (1 entity in total)
• 機能のキーワード: peptoid, n-substituted glycine, maculatin, antimicrobial peptide, antimicrobial protein
• 由来する生物種: Litoria genimaculata (Green-eyed tree frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2149.58

構造登録者

Uggerhoej, L.E.,Guentert, P.,Wimmer, R. (登録日: 2014-03-15, 公開日: 2014-07-23, 最終更新日: 2023-06-14)

主引用文献

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

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

実験手法

SOLUTION NMR