2gv2
From Proteopedia
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- | [[Image:2gv2.gif|left|200px]] | + | [[Image:2gv2.gif|left|200px]] |
- | + | ||
- | '''MDM2 in complex with an 8-mer p53 peptide analogue''' | + | {{Structure |
+ | |PDB= 2gv2 |SIZE=350|CAPTION= <scene name='initialview01'>2gv2</scene>, resolution 1.80Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= MDM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''MDM2 in complex with an 8-mer p53 peptide analogue''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2GV2 is a [ | + | 2GV2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV2 OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16925398 16925398] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:09:28 2008'' |
Revision as of 15:09, 20 March 2008
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, resolution 1.80Å | |||||||
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Ligands: | |||||||
Gene: | MDM2 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
MDM2 in complex with an 8-mer p53 peptide analogue
Overview
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 A 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 Structure
2GV2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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