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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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| Asıl Yazarlar: | , , , , , , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
2009
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| Konular: | |
| Online Erişim: | 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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