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PDBsum entry 1yiu
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References listed in PDB file
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Key reference
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Title
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Phosphorylation of either ser16 or thr30 does not disrupt the structure of the itch e3 ubiquitin ligase third ww domain.
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Authors
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A.Z.Shaw,
P.Martin-Malpartida,
B.Morales,
F.Yraola,
M.Royo,
M.J.Macias.
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Ref.
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Proteins, 2005,
60,
558-560.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. a: Itch-ww3 sequence. Two possible sites identified
by NetPhos 2.0 phosphorylation prediction server are indicated
in red. The immediate amino acid environment of Thr30 is typical
of a phosphorylation site for Casein kinase II, CK2, whereas
protein kinase A, PKA is predicted to phosphorylate both Thr30
and Ser16. b: A ribbon representation of Itch-ww3 domain showing
the side chains of conserved aromatic residues in magenta. Ser16
and Thr30 are displayed in gold. The stereo-view of the best-fit
backbone superposition of 10 NMR derived structures selected
according to the lowest energy is shown in the Supplementary
Material. The structures are displayed with MOLMOL.[20] c:
Selected region of 2D NOESY experiments carried out in D[2]O,
showing a characteristic pattern of  -
NOEs
found in the WW fold. 1 corresponds to T30-V23, 2 to K12-F22, 3
to N24-W10, and 4 T14-V20. A table containing the proton
chemical shifts of the three domains is given as Supplementary
Material.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
60,
558-560)
copyright 2005.
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