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1T4F

Structure of human MDM2 in complex with an optimized p53 peptide

Summary for 1T4F
Entry DOI10.2210/pdb1t4f/pdb
Related1RV1 1T4E 1YCR
DescriptorUbiquitin-protein ligase E3 Mdm2, optimized p53 peptide, SULFATE ION, ... (4 entities in total)
Functional Keywordsmdm2-p53 peptide complex, p53-binding protein mdm2 oncoprotein mdm2 double minute 2 protein hdm2, ligase
Biological sourceHomo sapiens (human)
Cellular locationNucleus, nucleoplasm: Q00987
Total number of polymer chains2
Total formula weight13905.84
Authors
Grasberger, B.L.,Schubert, C.,Koblish, H.K.,Carver, T.E.,Franks, C.F.,Zhao, S.Y.,Lu, T.,LaFrance, L.V.,Parks, D.J. (deposition date: 2004-04-29, release date: 2005-02-08, Last modification date: 2023-08-23)
Primary citationGrasberger, B.L.,Lu, T.,Schubert, C.,Parks, D.J.,Carver, T.E.,Koblish, H.K.,Cummings, M.D.,LaFrance, L.V.,Milkiewicz, K.L.
Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells
J.Med.Chem., 48:909-912, 2005
Cited by
PubMed Abstract: HDM2 binds to an alpha-helical transactivation domain of p53, inhibiting its tumor suppressive functions. A miniaturized thermal denaturation assay was used to screen chemical libraries, resulting in the discovery of a novel series of benzodiazepinedione antagonists of the HDM2-p53 interaction. The X-ray crystal structure of improved antagonists bound to HDM2 reveals their alpha-helix mimetic properties. These optimized molecules increase the transcription of p53 target genes and decrease proliferation of tumor cells expressing wild-type p53.
PubMed: 15715460
DOI: 10.1021/jm049137g
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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