2K98

Helical hairpin structure of potent antimicrobial peptide MSI-594 in the presence of Lipopolysaccharide micelle

2K98 の概要

• エントリーDOI: 10.2210/pdb2k98/pdb
• 分子名称: MSI-594 (1 entity in total)
• 機能のキーワード: msi-594, lps, trnoe, antimicrobial peptide, antimicrobial protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2447.10

構造登録者

Bhunia, A.,Bhattacharjya, S.,Ramamoorthy, A. (登録日: 2008-09-30, 公開日: 2009-02-10, 最終更新日: 2024-05-29)

主引用文献

Bhunia, A.,Ramamoorthy, A.,Bhattacharjya, S.
Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy
Chemistry, 15:2036-2040, 2009

PubMed Abstract: Essential understanding: Elucidation of structural requirements and interactions of antimicrobial peptides with lipopolysaccharide (LPS) are essential to understand the mechanism of action of antimicrobial peptides. The highly active antimicrobial peptide MSI-594 (see figure for electrostatic potential surface) acquires a novel helical hairpin structure in complex with LPS. The structure and interactions of MSI-594 with LPS presented here provide important insights into the mechanism of outer membrane permeabilization by antimicrobial peptides.

PubMed: 19180607
DOI: 10.1002/chem.200802635

実験手法

SOLUTION NMR