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PDBsum entry 2wh0
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Signaling protein
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PDB id
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2wh0
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Recognition of an intrachain tandem 14-3-3 binding site within protein kinasE C epsilon
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Structure:
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14-3-3 protein zeta/delta. Chain: a, b, c, d. Synonym: 14-3-3 zeta, kcip-1, protein kinasE C inhibitor protein 1. Engineered: yes. Protein kinasE C epsilon type, npkc-epsilon. Chain: q, r. Fragment: pkc epsilon v3-derived peptide, residues 342-372. Synonym: pkcev3. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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2.25Å
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R-factor:
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0.183
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R-free:
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0.235
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Authors:
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B.Kostelecky,A.T.Saurin,A.Purkiss,P.J.Parker,N.Q.Mcdonald
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Key ref:
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B.Kostelecky
et al.
(2009).
Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon.
Embo Rep,
10,
983-989.
PubMed id:
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Date:
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28-Apr-09
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Release date:
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18-Aug-09
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PROCHECK
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Headers
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References
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Enzyme class:
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Chain Q:
E.C.2.7.11.13
- protein kinase C.
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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 Rep
10:983-989
(2009)
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PubMed id:
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Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon.
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B.Kostelecky,
A.T.Saurin,
A.Purkiss,
P.J.Parker,
N.Q.McDonald.
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ABSTRACT
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The phosphoserine/threonine binding protein 14-3-3 stimulates the catalytic
activity of protein kinase C-epsilon (PKCepsilon) by engaging two tandem
phosphoserine-containing motifs located between the PKCepsilon regulatory and
catalytic domains (V3 region). Interaction between 14-3-3 and this region of
PKCepsilon is essential for the completion of cytokinesis. Here, we report the
crystal structure of 14-3-3zeta bound to a synthetic diphosphorylated PKCepsilon
V3 region revealing how a consensus 14-3-3 site and a divergent 14-3-3 site
cooperate to bind to 14-3-3 and so activate PKCepsilon. Thermodynamic data show
a markedly enhanced binding affinity for two-site phosphopeptides over
single-site 14-3-3 binding motifs and identifies Ser 368 as a gatekeeper
phosphorylation site in this physiologically relevant 14-3-3 ligand. This
dual-site intra-chain recognition has implications for other 14-3-3 targets,
which seem to have only a single 14-3-3 motif, as other lower affinity and
cryptic 14-3-3 gatekeeper sites might exist.
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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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R.J.Falconer,
and
B.M.Collins
(2011).
Survey of the year 2009: applications of isothermal titration calorimetry.
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J Mol Recognit,
24,
1.
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W.Mair,
I.Morantte,
A.P.Rodrigues,
G.Manning,
M.Montminy,
R.J.Shaw,
and
A.Dillin
(2011).
Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB.
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Nature,
470,
404-408.
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C.Johnson,
S.Crowther,
M.J.Stafford,
D.G.Campbell,
R.Toth,
and
C.MacKintosh
(2010).
Bioinformatic and experimental survey of 14-3-3-binding sites.
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Biochem J,
427,
69-78.
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M.Kaiser,
and
C.Ottmann
(2010).
The first small-molecule inhibitor of 14-3-3s: modulating the master regulator.
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Chembiochem,
11,
2085-2087.
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P.D.Adams,
P.V.Afonine,
G.Bunkóczi,
V.B.Chen,
I.W.Davis,
N.Echols,
J.J.Headd,
L.W.Hung,
G.J.Kapral,
R.W.Grosse-Kunstleve,
A.J.McCoy,
N.W.Moriarty,
R.Oeffner,
R.J.Read,
D.C.Richardson,
J.S.Richardson,
T.C.Terwilliger,
and
P.H.Zwart
(2010).
PHENIX: a comprehensive Python-based system for macromolecular structure solution.
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Acta Crystallogr D Biol Crystallogr,
66,
213-221.
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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.
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Links
