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
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DOI：
10.1002/prot.24048
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发表时间：
2012-03-01
影响因子：
2.9
通讯作者：
Spyroulias, Georgios A.
中科院分区：
文献类型：
--
作者：
Chasapis, Christos T.;Kandias, Nikolaos G.;Spyroulias, Georgios A.
Arkadia（Rnf 111）是一种E3泛素（Ub）连接酶，通过靶向降解负调节因子Smad 6/7和SnoN/Ski转录抑制因子（当它们阻断TGF-β效应因子Smad 2/3时）来放大TGF-β信号传导反应。Arkadia的E3连接酶活性取决于其C-末端RING-H2结构域，该结构域构成携带活化Ub的E2 Ub缀合酶的对接位点。我们确定了Arkadia的RING-H2结构域的核磁共振溶液结构，并揭示了一个（beta）a折叠，与预期的Zn（II）-连接的交叉支撑模式完全一致。此外，Arkadia RING-H2结构域与其E2伴侣酶（UbcH 5 b）的相互作用通过化学位移扰动进行了检查。Proteins 2012. (c)2012 Wiley Periodicals，Inc.
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'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. (c) 2012 Wiley Periodicals, Inc.