2gv2: Difference between revisions
New page: left|200px<br /> <applet load="2gv2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gv2, resolution 1.80Å" /> '''MDM2 in complex wit... |
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[[Image:2gv2.gif|left|200px]]<br /> | [[Image:2gv2.gif|left|200px]]<br /><applet load="2gv2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2gv2, resolution 1.80Å" /> | caption="2gv2, resolution 1.80Å" /> | ||
'''MDM2 in complex with an 8-mer p53 peptide analogue'''<br /> | '''MDM2 in complex with an 8-mer p53 peptide analogue'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2GV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2GV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: optimized protein-protein interaction. synthetic peptide. alpha helix binding protein]] | [[Category: optimized protein-protein interaction. synthetic peptide. alpha helix binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:29:12 2008'' | ||
Revision as of 18:29, 15 February 2008
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MDM2 in complex with an 8-mer p53 peptide analogue
OverviewOverview
The most potent inhibitor of the p53-MDM2 interaction reported to date is an 8-mer p53 peptide analogue (Novartis peptide), which contains 6-chlorotryptophane (Cl-Trp) and phosphonomethylphenylalanine (Pmp) as key residues for the enhanced activity. We report here a crystal structure of the co-complex between MDM2 and the Novartis peptide solved at 1.8 Å resolution. The structural basis for the role of the two aromatic residues are delineated by comparing the present structure with crystal structures of the MDM2 co-complex bound to other inhibitors including the wt-p53 peptide itself.
About this StructureAbout this Structure
2GV2 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic analysis of an 8-mer p53 peptide analogue complexed with MDM2., Sakurai K, Schubert C, Kahne D, J Am Chem Soc. 2006 Aug 30;128(34):11000-1. PMID:16925398
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