1t4e

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{{STRUCTURE_1t4e| PDB=1t4e | SCENE= }}
{{STRUCTURE_1t4e| PDB=1t4e | SCENE= }}
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'''Structure of Human MDM2 in complex with a Benzodiazepine Inhibitor'''
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===Structure of Human MDM2 in complex with a Benzodiazepine Inhibitor===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15715460 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15715460}}
==About this Structure==
==About this Structure==
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[[Category: Zhao, S Y.]]
[[Category: Zhao, S Y.]]
[[Category: Mdm2-inhibitor complex]]
[[Category: Mdm2-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:30:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:11:34 2008''

Revision as of 17:11, 27 July 2008

Image:1t4e.png

Template:STRUCTURE 1t4e

Structure of Human MDM2 in complex with a Benzodiazepine Inhibitor

Template:ABSTRACT PUBMED 15715460

About this Structure

1T4E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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