2k98

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

spinqualitylabelsall models 2k98, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k98 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy.,Bhunia A, Ramamoorthy A, Bhattacharjya S Chemistry. 2009 Jan 29;15(9):2036-2040. PMID:19180607 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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