1T4F: Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide

Citation:
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.
PDB ID: 1T4FDownload
MMDB ID: 31805
PDB Deposition Date: 2004/4/29
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1T4F: dimeric; determined by author and by software (PISA)
Molecular Components in 1T4F
Label Count Molecule
Proteins (2 molecules)
1
Ubiquitin-protein Ligase E3 Mdm2(Gene symbol: MDM2)
Molecule annotation
1
Optimized P53 Peptide
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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