3LNJ

Crystal structure of human MDM2 in complex with D-peptide inhibitor (DPMI-alpha)

Summary for 3LNJ

Entry DOI	10.2210/pdb3lnj/pdb
Related	1YCR 3EQS 3IUX 3IWY
Related PRD ID	PRD_000808
Descriptor	E3 ubiquitin-protein ligase Mdm2, D-peptide inhibitor, SULFATE ION, ... (6 entities in total)
Functional Keywords	mdm2, p53 binding domain, d-peptide activator of mdm2, mdm2-d-peptide complex, host-virus interaction, ligase, metal-binding, nucleus, phosphoprotein, proto-oncogene, ubl conjugation pathway, zinc-finger, ligase-ligase inhibitor complex, ligase/ligase inhibitor
Cellular location	Nucleus, nucleoplasm: Q00987
Total number of polymer chains	6
Total formula weight	34923.50
Authors	Pazgier, M.,Lu, W. (deposition date: 2010-02-02, release date: 2010-03-09, Last modification date: 2024-11-06)
Primary citation	Liu, M.,Pazgier, M.,Li, C.,Yuan, W.,Li, C.,Lu, W. A left-handed solution to peptide inhibition of the p53-MDM2 interaction. Angew.Chem.Int.Ed.Engl., 49:3649-3652, 2010 Cited by PubMed Abstract: [Image: see text] The oncoprotein MDM2 negatively regulates the activity and stability of the tumor suppressor protein p53, and is an important molecular target for anticancer therapy. Mirror image phage display identifies a high-affinity D-peptide ligand of MDM2 that can be developed into a potent and protease-resistant p53 activator with potential antitumor activity. PubMed: 20449836 DOI: 10.1002/anie.201000329 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation