3ng2 | pdb_00003ng2

Crystal structure of the RNF4 ring domain dimer

spinqualitylabelsall models 3ng2, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ng2 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, ZN Gene: Rnf4 (Rattus norvegicus) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization. RING domain dimerization is essential for RNF4 function.,Liew CW, Sun H, Hunter T, Day CL Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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