2kiz | pdb_00002kiz
Solution structure of Arkadia RING-H2 finger domain
Structural highlights
Function[RN111_HUMAN] Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin-protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Associates with UBE2D2 as an E2 enzyme.[1] [2] [3] [4] 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 PubMedArkadia (Rnf111), an E3 Ubiquitin (Ub) ligase, amplifies TGF-beta signaling responses by targeting for degradation of the negative regulators Smad6/7 and the SnoN/Ski transcriptional repressors when they block the TGF-beta 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 (beta)betabetaalpha 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. (c) 2012 Wiley Periodicals, Inc. NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase.,Chasapis CT, Kandias NG, Episkopou V, Bentrop D, Spyroulias GA Proteins. 2012 May;80(5):1484-9. doi: 10.1002/prot.24048. Epub 2012 Mar 13. PMID:22411132[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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