2KIZ
Solution structure of Arkadia RING-H2 finger domain
Summary for 2KIZ
| Entry DOI | 10.2210/pdb2kiz/pdb |
| NMR Information | BMRB: 15948 |
| Descriptor | E3 ubiquitin-protein ligase Arkadia, ZINC ION (2 entities in total) |
| Functional Keywords | arkadia, ring-h2 finger, e3 ligase, zn binding domain, metal-binding, zinc-finger, metal binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q6ZNA4 |
| Total number of polymer chains | 1 |
| Total formula weight | 8090.85 |
| Authors | Kandias, N.G.,Chasapis, C.T.,Bentrop, D.,Episkopou, V.,Spyroulias, G.A. (deposition date: 2009-05-13, release date: 2010-05-19, Last modification date: 2024-11-06) |
| Primary citation | Chasapis, C.T.,Kandias, N.G.,Episkopou, V.,Bentrop, D.,Spyroulias, G.A. NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase. Proteins, 80:1484-1489, 2012 Cited by PubMed Abstract: Arkadia (Rnf111), an E3 Ubiquitin (Ub) ligase, amplifies TGF-β signaling responses by targeting for degradation of the negative regulators Smad6/7 and the SnoN/Ski transcriptional repressors when they block the TGF-β effectors Smad2/3. The E3 ligase activity of Arkadia depends on its C-terminal RING-H2 domain that constitutes the docking site for the E2 Ub-conjugating enzyme carrying the activated Ub. We determined the nuclear magnetic resonance solution structure of Arkadia's RING-H2 domain and revealed a (β)ββα fold, fully consistent with the expected "cross-brace" mode of Zn(II)-ligation. In addition, the interaction of the Arkadia RING-H2 domain with its E2 partner enzyme (UbcH5b) was examined through chemical shift perturbation. Proteins 2012. © 2012 Wiley Periodicals, Inc. PubMed: 22411132DOI: 10.1002/prot.24048 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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