MDM4

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Line 8: Line 8:
[[2cr8]] – hMDM4 ZF-RNBP domain – NMR<br />
[[2cr8]] – hMDM4 ZF-RNBP domain – NMR<br />
-
[[3dab]] – hMDM4 + p53 transactivation domain<br />
+
[[3dab]], [[2mwy]] – hMDM4 SWIB domain + p53 transactivation domain<br />
 +
[[2n06]], [[2n0u]], [[2n0w]], [[2n14]] – hMDM4 SWIB domain + p53 transactivation domain – NMR<br />
[[3fdo]], [[3jzo]], [[3jzp]], [[3jzq]], [[3jzr]], [[3jzs]] – hMDM4 p53-binding domain + peptide<br />
[[3fdo]], [[3jzo]], [[3jzp]], [[3jzq]], [[3jzr]], [[3jzs]] – hMDM4 p53-binding domain + peptide<br />
[[3lbj]] - hMDM4 p53-binding domain + inhibitor<br />
[[3lbj]] - hMDM4 p53-binding domain + inhibitor<br />

Revision as of 06:56, 20 April 2016

Template:STRUCTURE 3jzo

MDM4 is a 490 amino acid protein containing a RING finger domain and a nuclear localization signal. MDM4 interacts with protein MDM2[1]. Both of these proteins show structure similarity and contain a p53-binding domain in their N terminal.

3D Structures of MDM4

Updated on 20-April-2016

2cr8 – hMDM4 ZF-RNBP domain – NMR
3dab, 2mwy – hMDM4 SWIB domain + p53 transactivation domain
2n06, 2n0u, 2n0w, 2n14 – hMDM4 SWIB domain + p53 transactivation domain – NMR
3fdo, 3jzo, 3jzp, 3jzq, 3jzr, 3jzs – hMDM4 p53-binding domain + peptide
3lbj - hMDM4 p53-binding domain + inhibitor
3u15 - hMDM4 p53-binding domain + indolyl hydantoin
3dac – hMDM4 (mutant) + p53 transactivation domain
2vyr – hMDM4 N terminal + antibody
3fe7, 3fea, 3eqy - hMDM4 N terminal (mutant) + peptide
2vje, 2vjf – hMDM2 residues 383-446 + hMDM4 residues 428-490
2z5s - zMDM4 SWIB domain + p53 transactivation domain – zebrafish
2z5t - zMDM4 SWIB domain (mutant) + p53 transactivation domain
4n5t - zMDM4 SWIB domain (mutant) + stapled peptide

References

  1. ↑ Migliorini D, Lazzerini Denchi E, Danovi D, Jochemsen A, Capillo M, Gobbi A, Helin K, Pelicci PG, Marine JC. Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development. Mol Cell Biol. 2002 Aug;22(15):5527-38. PMID:12101245

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

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