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Title: Fragmenting the S100B-p53 Interaction: Combined Virtual/Biophysical Screening Approaches to Identify Ligands
Authors: M., Agamennone
L., Cesari
D., Lalli
E., Turlizzi
R. D., Conte
P., Turano
Mangani, Stefano 
A., Padova
Keywords: x-ray; crystal structure; s100beta; inhibitor; protein-protein interaction
Issue Date: 2010
Project: None 
S100B contributes to cell proliferation by binding the C terminus of p53 and inhibiting its tumor suppressor function. The use of multiple computational approaches to screen fragment libraries targeting the human S100B-p53 interaction site is reported. This in silico screening led to the identification of 280 novel prospective ligands. NMR spectroscopic experiments revealed specific binding at the p53 interaction site for a set of these compounds and confirmed their potential for further rational optimization. The X-ray crystal structure determined for one of the binders revealed key intermolecular interactions, thus paving the way for structure-based ligand optimization.
ISSN: 1860-7179
DOI: 10.1002/cmdc.200900393
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