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PDBsum entry 1nxk
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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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Catalytically active map kap kinase 2 structures in complex with staurosporine and ADP reveal differences with the autoinhibited enzyme.
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Authors
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K.W.Underwood,
K.D.Parris,
E.Federico,
L.Mosyak,
R.M.Czerwinski,
T.Shane,
M.Taylor,
K.Svenson,
Y.Liu,
C.L.Hsiao,
S.Wolfrom,
M.Maguire,
K.Malakian,
J.B.Telliez,
L.L.Lin,
R.W.Kriz,
J.Seehra,
W.S.Somers,
M.L.Stahl.
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Ref.
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Structure, 2003,
11,
627-636.
[DOI no: ]
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PubMed id
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Abstract
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MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the
inflammatory process. We have determined the crystal structures of a
catalytically active C-terminal deletion form of human MK2, residues 41-364, in
complex with staurosporine at 2.7 A and with ADP at 3.2 A, revealing overall
structural similarity with other Ser/Thr kinases. Kinetic analysis reveals that
the K(m) for ATP is very similar for MK2 41-364 and p38-activated MK2 41-400.
Conversely, the catalytic rate and binding for peptide substrate are
dramatically reduced in MK2 41-364. However, phosphorylation of MK2 41-364 by
p38 restores the V(max) and K(m) for peptide substrate to values comparable to
those seen in p38-activated MK2 41-400, suggesting a mechanism for regulation of
enzyme activity.
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Figure 4.
Figure 4. Comparison of Ser/Thr KinasesRibbons
representation of (A) MK2 41-364, (B) MK2 47-400 (Protein Data
Bank ID 1KWP), (C) titan kinase (1TKI), (D) camp-dependent
kinase (1ATP), and (E) Ca^2+/calmodulin-dependent kinase (1A06).
Each structure is depicted in approximately the same
orientation; autoinhibitory domain, red. The figures were
generated with Ribbons (Carson, 1997).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
627-636)
copyright 2003.
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