1t4f

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Structure of human MDM2 in complex with an optimized p53 peptide

File:1t4f.gif


1t4f, resolution 1.90Å

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OverviewOverview

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.

About this StructureAbout this Structure

1T4F is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells., Grasberger BL, Lu T, Schubert C, Parks DJ, Carver TE, Koblish HK, Cummings MD, LaFrance LV, Milkiewicz KL, Calvo RR, Maguire D, Lattanze J, Franks CF, Zhao S, Ramachandren K, Bylebyl GR, Zhang M, Manthey CL, Petrella EC, Pantoliano MW, Deckman IC, Spurlino JC, Maroney AC, Tomczuk BE, Molloy CJ, Bone RF, J Med Chem. 2005 Feb 24;48(4):909-12. PMID:15715460

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