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PDBsum entry 2dq7
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.10.2
- non-specific protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochem Biophys Res Commun
346:840-844
(2006)
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PubMed id:
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Structure of human Fyn kinase domain complexed with staurosporine.
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T.Kinoshita,
M.Matsubara,
H.Ishiguro,
K.Okita,
T.Tada.
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ABSTRACT
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The tyrosine kinase Fyn is a member of the Src kinase family. Besides the role
of Fyn in T cell signal transduction in concert with Lck, its excess activity in
the brain is involved with conditions such as Alzheimer's and Parkinson's
diseases. Therefore, inhibition of Fyn kinase may help counteract these nervous
system disorders. Here, we solved the crystal structure of the human Fyn kinase
domain complexed with staurosporine, a potent kinase inhibitor, at 2.8 A
resolution. Staurosporine binds to the ATP-binding site of Fyn in a similar
manner as in the Lck- and Csk-complexes. The small structural differences in the
staurosporine-binding and/or -unbinding region among the three kinase domains
may help obtaining the selective inhibitors against the respective kinases.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.C.Lee,
Y.Jia,
N.Li,
X.Sun,
K.Ng,
E.Ambing,
M.Y.Gao,
S.Hua,
C.Chen,
S.Kim,
P.Y.Michellys,
S.A.Lesley,
J.L.Harris,
and
G.Spraggon
(2010).
Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain.
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Biochem J,
430,
425-437.
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PDB codes:
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O.A.Gani,
and
R.A.Engh
(2010).
Protein kinase inhibition of clinically important staurosporine analogues.
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Nat Prod Rep,
27,
489-498.
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X.Yang,
T.Kinoshita,
M.Gouda,
K.Yokota,
and
T.Tada
(2010).
A silent mutation made possible efficient production of active human Frk tyrosine kinase in Escherichia coli.
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Biosci Biotechnol Biochem,
74,
125-128.
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M.A.Meyn,
and
T.E.Smithgall
(2009).
Chemical genetics identifies c-Src as an activator of primitive ectoderm formation in murine embryonic stem cells.
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Sci Signal,
2,
ra64.
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R.Barouch-Bentov,
J.Che,
C.C.Lee,
Y.Yang,
A.Herman,
Y.Jia,
A.Velentza,
J.Watson,
L.Sternberg,
S.Kim,
N.Ziaee,
A.Miller,
C.Jackson,
M.Fujimoto,
M.Young,
S.Batalov,
Y.Liu,
M.Warmuth,
T.Wiltshire,
M.P.Cooke,
and
K.Sauer
(2009).
A conserved salt bridge in the G loop of multiple protein kinases is important for catalysis and for in vivo Lyn function.
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Mol Cell,
33,
43-52.
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S.W.Cowan-Jacob,
G.Fendrich,
A.Floersheimer,
P.Furet,
J.Liebetanz,
G.Rummel,
P.Rheinberger,
M.Centeleghe,
D.Fabbro,
and
P.W.Manley
(2007).
Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia.
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Acta Crystallogr D Biol Crystallogr,
63,
80-93.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
