Jan 25, 2008 · Here we report the crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 (UbcH5b). In both MDM2 and MDMX residues...

Here we report the crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 (UbcH5b). In both MDM2 and MDMX residues C-terminal to the RING domain have a key role in dimer formation.

Mar 5, 2021 · The unit cell for the MDM2 z crystal contains two molecules of MDM2 z, which form a dimer. The overall structure is similar to MDM2 h (RMSD of 0.6 Å), where all secondary structure elements and the coordination of zinc ions are conserved (Figure 2 (a)).

May 29, 2017 · Guided by a novel crystal structure of the MDM2–MDMX–E2(UbcH5B)–ubiquitin complex, we designed MDM2 mutants that prevent E2–ubiquitin binding without altering the RING-domain structure.

Background: MDM2 dimerization is required for p53 ubiquitination and degradation. Results: MDM2-MDM2 and MDM2-MDMX interactions occur through different mechanisms. Conclusion: MDM2-MDMX interaction requires the proper MDM2 RING domain structure, ...

MDM2 binds the transactivation domain of p53 and inhibits the ability of p53 to activate transcription. Importantly, MDM2 binding also promotes the ubiquitin-mediated degradation of p53, as well as the export of p53 from the nucleus to the cytoplasm.

In cell-based assays, MDM2 exhibits superior binding to, hyperdegradation of, and increased nuclear exclusion of dimeric p53 when compared with tetrameric wild-type p53. Correspondingly, impairing the hydrophobicity of the newly identified N-terminal MDM2 region leads to …

Here we report the crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 (UbcH5b). In both MDM2 and MDMX residues...

Dec 10, 2007 · Here we report the crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 (UbcH5b). In both MDM2 and MDMX residues C-terminal to the RING domain have a key role in dimer formation.

Using chemical cross-linking, we show that the MDM2 RING domain forms oligomers including dimer and higher-order complexes in vivo. RING domain dimerization efficiency is negatively regulated by upstream sequence.