3IUX

Crystal structure of human MDM2 in complex with a potent miniature protein inhibitor (18-residues)

Summary for 3IUX

Entry DOI	10.2210/pdb3iux/pdb
Related	1T4E 1YCR 3EQY 3IVJ
Descriptor	E3 ubiquitin-protein ligase Mdm2, miniature protein inhibitor, ACETATE ION, ... (5 entities in total)
Functional Keywords	mdm2, p53 binding domain, peptide activator of p53, host-virus interaction, ligase, metal-binding, nucleus, phosphoprotein, proto-oncogene, ubl conjugation pathway, zinc-finger
Cellular location	Nucleus, nucleoplasm: Q00987
Total number of polymer chains	4
Total formula weight	24806.53
Authors	Pazgier, M.,Lu, W. (deposition date: 2009-08-31, release date: 2009-10-27, Last modification date: 2023-09-06)
Primary citation	Li, C.,Pazgier, M.,Liu, M.,Lu, W.Y.,Lu, W. Apamin as a template for structure-based rational design of potent peptide activators of p53. Angew.Chem.Int.Ed.Engl., 48:8712-8715, 2009 Cited by PubMed Abstract: [Image: see text] The oncoproteins MDM2 and MDMX negatively regulate the activity and stability of the tumor suppressor protein p53, and are important molecular targets for anticancer therapy. Grafting four residues critical for MDM2/MDMX binding to the C-terminal α-helix of apamin converts the bee-venom neurotoxin into a novel class of potent p53 activators with potential antitumor activity. PubMed: 19827079 DOI: 10.1002/anie.200904550 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.65 Å)

Structure validation