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NMR‐based insights into the conformational and interaction properties of Arkadia RING‐H2 E3 Ub ligase
Author(s) -
Chasapis Christos T.,
Kandias Nikolaos G.,
Episkopou Vasso,
Bentrop Detlef,
Spyroulias Georgios A.
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24048
Subject(s) - ubiquitin ligase , chemistry , dna ligase , ubiquitin , docking (animal) , ubiquitin protein ligases , stereochemistry , crystallography , enzyme , biochemistry , medicine , nursing , gene
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.