1z64
From Proteopedia
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NMR Solution Structure of Pleurocidin in DPC Micelles
Overview
Pleurocidin is an antimicrobial peptide that was isolated from the mucus membranes of winter flounder (Pseudopleuronectes americanus) and contributes to the initial stages of defense against bacterial infection. From NMR structural studies with the uniformly (15)N-labeled peptide, a structure of pleurocidin was determined to be in a random coil conformation in aqueous solution whereas it assumes an alpha-helical structure in TFE and in dodecylphosphocholine (DPC) micelles. From (15)N relaxation studies, the helix is a rigid structure in the membrane-mimicking environment. Strong NOESY cross-peaks from the pleurocidin to the aliphatic chain on DPC confirm that pleurocidin is contained within the DPC micelle and not associated with the surface of the micelle. From diffusion studies it was determined that each micelle contains at least two pleurocidin molecules.
About this Structure
1Z64 is a Single protein structure of sequence from Pseudopleuronectes americanus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural characterization of the antimicrobial peptide pleurocidin from winter flounder., Syvitski RT, Burton I, Mattatall NR, Douglas SE, Jakeman DL, Biochemistry. 2005 May 17;44(19):7282-93. PMID:15882067
Page seeded by OCA on Thu Feb 21 16:12:27 2008
