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PDBsum entry 1i09
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of gsk3beta reveals a primed phosphorylation mechanism.
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Authors
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E.Ter haar,
J.T.Coll,
D.A.Austen,
H.M.Hsiao,
L.Swenson,
J.Jain.
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Ref.
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Nat Struct Biol, 2001,
8,
593-596.
[DOI no: ]
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PubMed id
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Abstract
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GSK3beta was identified as the kinase that phosphorylates glycogen synthase but
is now known to be involved in multiple signaling pathways. GSK3beta prefers
prior phosphorylation of its substrates. We present the structure of
unphosphorylated GSK3beta at 2.7 A. The orientation of the two domains and
positioning of the activation loop of GSK3beta are similar to those observed in
activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies
the same position as the phosphate group of the phosphothreonine in activated
p38gamma, CDK2 or ERK2. A loop from a neighboring molecule in the crystal
occupies a portion of the substrate binding groove. The structure explains the
unique primed phosphorylation mechanism of GSK3beta and how GSK3beta relies on a
phosphoserine in the substrate for the alignment of the beta- and alpha-helical
domains.
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Figure 1.
Figure 1. Representative portion of a 2F[o] - F[c] electron
density map contoured at 1.5  .
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Figure 4.
Figure 4. The GSK3  substrate
binding groove.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
593-596)
copyright 2001.
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