Small Molecules Bound to Unique Sites in the Target Protein Binding Cleft of Calcium-Bound S100B As Characterized by Nuclear Magnetic Resonance and X-ray Crystallography

Structural studies are part of a rational drug design program aimed at inhibiting the S100B–p53 interaction and restoring wild-type p53 function in malignant melanoma. To this end, structures of three compounds (SBi132, SBi1279, and SBi523) bound to Ca(2+)-S100B were determined by X-ray crystallogra...

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Main Authors: Charpentier, Thomas H., Wilder, Paul T., Liriano, Melissa A., Varney, Kristen M., Zhong, Shijun, Coop, Andrew, Pozharski, Edwin, MacKerell, Alexander D., Toth, Eric A., Weber, David J.
Format: Artigo
Language:Inglês
Published: 2009
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Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2804263/
https://ncbi.nlm.nih.gov/pubmed/19469484
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi9005754
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