NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase

作者：Chasapis Christos T; Kandias Nikolaos G; Episkopou Vasso; Bentrop Detlef; Spyroulias Georgios A^*

来源：Proteins: Structure, Function, and Genetics , 2012, 80(5): 1484-1489.

DOI：10.1002/prot.24048

• Arkadia
• Rnf111
• E3 ubiquitin ligase
• RING finger domain
• TGF-ss
• UbcH5b E2 enzyme
• NMR

Arkadia (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%26apos;s RING-H2 domain and revealed a (beta)a 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.

• 出版日期2012-3