1. Academic Validation
  2. NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase

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

  • Proteins. 2012 May;80(5):1484-9. doi: 10.1002/prot.24048.
Christos T Chasapis 1 Nikolaos G Kandias Vasso Episkopou Detlef Bentrop Georgios A Spyroulias
Affiliations

Affiliation

  • 1 Department of Pharmacy, University of Patras, Patras GR-26504, Greece.
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.

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