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PDBsum entry 1koa
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[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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Embo J
15:6810-6821
(1996)
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PubMed id:
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Giant protein kinases: domain interactions and structural basis of autoregulation.
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B.Kobe,
J.Heierhorst,
S.C.Feil,
M.W.Parker,
G.M.Benian,
K.R.Weiss,
B.E.Kemp.
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ABSTRACT
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The myosin-associated giant protein kinases twitchin and titin are composed
predominantly of fibronectin- and immunoglobulin-like modules. We report the
crystal structures of two autoinhibited twitchin kinase fragments, one from
Aplysia and a larger fragment from Caenorhabditis elegans containing an
additional C-terminal immunoglobulin-like domain. The structure of the longer
fragment shows that the immunoglobulin domain contacts the protein kinase domain
on the opposite side from the catalytic cleft, laterally exposing potential
myosin binding residues. Together, the structures reveal the cooperative
interactions between the autoregulatory region and the residues from the
catalytic domain involved in protein substrate binding, ATP binding, catalysis
and the activation loop, and explain the differences between the observed
autoinhibitory mechanism and the one found in the structure of
calmodulin-dependent kinase I.
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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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T.M.Butler,
and
M.J.Siegman
(2011).
A force-activated kinase in a catch smooth muscle.
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J Muscle Res Cell Motil,
31,
349-358.
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Y.Mabuchi,
K.Mabuchi,
W.F.Stafford,
and
Z.Grabarek
(2010).
Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications.
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Biochemistry,
49,
2903-2917.
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D.N.Greene,
T.Garcia,
R.B.Sutton,
K.M.Gernert,
G.M.Benian,
and
A.F.Oberhauser
(2008).
Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains.
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Biophys J,
95,
1360-1370.
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R.Jauch,
M.K.Cho,
S.Jäkel,
C.Netter,
K.Schreiter,
B.Aicher,
M.Zweckstetter,
H.Jäckle,
and
M.C.Wahl
(2006).
Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment.
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EMBO J,
25,
4020-4032.
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PDB codes:
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A.G.Cook,
L.N.Johnson,
and
J.M.McDonnell
(2005).
Structural characterization of Ca2+/CaM in complex with the phosphorylase kinase PhK5 peptide.
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FEBS J,
272,
1511-1522.
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F.Gräter,
J.Shen,
H.Jiang,
M.Gautel,
and
H.Grubmüller
(2005).
Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations.
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Biophys J,
88,
790-804.
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M.Marino,
D.I.Svergun,
L.Kreplak,
P.V.Konarev,
B.Maco,
D.Labeit,
and
O.Mayans
(2005).
Poly-Ig tandems from I-band titin share extended domain arrangements irrespective of the distinct features of their modular constituents.
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J Muscle Res Cell Motil,
26,
355-365.
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S.Cheek,
K.Ginalski,
H.Zhang,
and
N.V.Grishin
(2005).
A comprehensive update of the sequence and structure classification of kinases.
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BMC Struct Biol,
5,
6.
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T.M.Ferrara,
D.B.Flaherty,
and
G.M.Benian
(2005).
Titin/connectin-related proteins in C. elegans: a review and new findings.
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J Muscle Res Cell Motil,
26,
435-447.
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A.Yamakawa,
H.Ogata,
K.Morita,
N.Shibata,
N.Andou,
H.Sanuki,
K.Yamada,
T.Hioki,
T.Ishii,
and
Y.Higuchi
(2004).
Crystallization and preliminary X-ray analysis of two inhibitor complexes of the catalytic domain of death-associated protein kinase.
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Acta Crystallogr D Biol Crystallogr,
60,
764-766.
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J.F.Harper,
G.Breton,
and
A.Harmon
(2004).
Decoding Ca(2+) signals through plant protein kinases.
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Annu Rev Plant Biol,
55,
263-288.
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M.Y.Niv,
H.Rubin,
J.Cohen,
L.Tsirulnikov,
T.Licht,
A.Peretzman-Shemer,
E.Cna'an,
A.Tartakovsky,
I.Stein,
S.Albeck,
I.Weinstein,
M.Goldenberg-Furmanov,
D.Tobi,
E.Cohen,
M.Laster,
S.A.Ben-Sasson,
and
H.Reuveni
(2004).
Sequence-based design of kinase inhibitors applicable for therapeutics and target identification.
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J Biol Chem,
279,
1242-1255.
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N.Fernandez-Fuentes,
A.Hermoso,
J.Espadaler,
E.Querol,
F.X.Aviles,
and
B.Oliva
(2004).
Classification of common functional loops of kinase super-families.
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Proteins,
56,
539-555.
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O.Rey,
J.R.Reeve,
E.Zhukova,
J.Sinnett-Smith,
and
E.Rozengurt
(2004).
G protein-coupled receptor-mediated phosphorylation of the activation loop of protein kinase D: dependence on plasma membrane translocation and protein kinase Cepsilon.
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J Biol Chem,
279,
34361-34372.
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J.Stamos,
M.X.Sliwkowski,
and
C.Eigenbrot
(2002).
Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor.
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J Biol Chem,
277,
46265-46272.
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PDB codes:
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O.Mayans,
J.Wuerges,
S.Canela,
M.Gautel,
and
M.Wilmanns
(2001).
Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.
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Structure,
9,
331-340.
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PDB code:
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V.Tereshko,
M.Teplova,
J.Brunzelle,
D.M.Watterson,
and
M.Egli
(2001).
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression.
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Nat Struct Biol,
8,
899-907.
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PDB codes:
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S.Hakeda,
S.Endo,
and
K.Saigo
(2000).
Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila.
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J Cell Biol,
148,
101-114.
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D.A.Enke,
P.Kaldis,
J.K.Holmes,
and
M.J.Solomon
(1999).
The CDK-activating kinase (Cak1p) from budding yeast has an unusual ATP-binding pocket.
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J Biol Chem,
274,
1949-1956.
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S.S.Taylor,
E.Radzio-Andzelm,
Madhusudan,
X.Cheng,
L.Ten Eyck,
and
N.Narayana
(1999).
Catalytic subunit of cyclic AMP-dependent protein kinase: structure and dynamics of the active site cleft.
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Pharmacol Ther,
82,
133-141.
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G.Zhi,
S.M.Abdullah,
and
J.T.Stull
(1998).
Regulatory segments of Ca2+/calmodulin-dependent protein kinases.
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J Biol Chem,
273,
8951-8957.
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H.Mehenni,
C.Gehrig,
J.Nezu,
A.Oku,
M.Shimane,
C.Rossier,
N.Guex,
J.L.Blouin,
H.S.Scott,
and
S.E.Antonarakis
(1998).
Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity.
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Am J Hum Genet,
63,
1641-1650.
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J.Szczepanowska,
U.Ramachandran,
C.J.Herring,
J.M.Gruschus,
J.Qin,
E.D.Korn,
and
H.Brzeska
(1998).
Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase.
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Proc Natl Acad Sci U S A,
95,
4146-4151.
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R.Littlefield,
and
V.M.Fowler
(1998).
Defining actin filament length in striated muscle: rulers and caps or dynamic stability?
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Annu Rev Cell Dev Biol,
14,
487-525.
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T.A.Millward,
C.W.Heizmann,
B.W.Schäfer,
and
B.A.Hemmings
(1998).
Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins.
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EMBO J,
17,
5913-5922.
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B.Kobe,
I.G.Jennings,
C.M.House,
S.C.Feil,
B.J.Michell,
T.Tiganis,
M.W.Parker,
R.G.Cotton,
and
B.E.Kemp
(1997).
Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase.
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Protein Sci,
6,
1352-1357.
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D.L.Silver,
A.V.Vorotnikov,
D.M.Watterson,
V.P.Shirinsky,
and
J.R.Sellers
(1997).
Sites of interaction between kinase-related protein and smooth muscle myosin.
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J Biol Chem,
272,
25353-25359.
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J.Heierhorst,
R.J.Mann,
and
B.E.Kemp
(1997).
Interaction of the recombinant S100A1 protein with twitchin kinase, and comparison with other Ca2+-binding proteins.
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Eur J Biochem,
249,
127-133.
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S.S.Taylor,
and
E.Radzio-Andzelm
(1997).
Protein kinase inhibition: natural and synthetic variations on a theme.
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Curr Opin Chem Biol,
1,
219-226.
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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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}
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