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-Structure paper
Title | Discovery of a novel class of highly potent inhibitors of the p53-MDM2 interaction by structure-based design starting from a conformational argument. |
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Journal, issue, pages | Bioorg. Med. Chem. Lett., Vol. 26, Page 4837-4841, Year 2016 |
Publish date | Aug 2, 2016 (structure data deposition date) |
Authors | Furet, P. / Masuya, K. / Kallen, J. / Stachyra-Valat, T. / Ruetz, S. / Guagnano, V. / Holzer, P. / Mah, R. / Stutz, S. / Vaupel, A. ...Furet, P. / Masuya, K. / Kallen, J. / Stachyra-Valat, T. / Ruetz, S. / Guagnano, V. / Holzer, P. / Mah, R. / Stutz, S. / Vaupel, A. / Chene, P. / Jeay, S. / Schlapbach, A. |
External links | Bioorg. Med. Chem. Lett. / PubMed:27542305 |
Methods | X-ray diffraction |
Resolution | 1.58 Å |
Structure data | PDB-5ln2: |
Chemicals | ChemComp-6ZT: ChemComp-SO4: ChemComp-CL: ChemComp-HOH: |
Source |
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Keywords | CELL CYCLE / PPI with p53 / inhibitor complex |