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PDBsum entry 2kiz
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Metal binding protein
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PDB id
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2kiz
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References listed in PDB file
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Key reference
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Title
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Nmr-Based insights into the conformational and interaction properties of arkadia ring-H2 e3 ub ligase.
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Authors
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C.T.Chasapis,
N.G.Kandias,
V.Episkopou,
D.Bentrop,
G.A.Spyroulias.
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Ref.
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Proteins, 2012,
80,
1484-1489.
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PubMed id
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Abstract
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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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Secondary reference #1
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Title
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High yield expression and nmr characterization of arkadia e3 ubiquitin ligase ring-H2 finger domain.
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Authors
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N.G.Kandias,
C.T.Chasapis,
D.Bentrop,
V.Episkopou,
G.A.Spyroulias.
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Ref.
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Biochem Biophys Res Commun, 2009,
378,
498-502.
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PubMed id
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