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PDBsum entry 2fk9
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Human protein kinasE C, eta
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Structure:
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Protein kinasE C, eta type. Chain: a. Fragment: c2 domain (residues 1-138). Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: prkch. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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1.75Å
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R-factor:
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0.180
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R-free:
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0.215
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Authors:
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J.R.Walker,D.R.Littler,P.J.Finerty Jr.,F.Mackenzie,E.M.Newman, J.Weigelt,M.Sundstrom,C.Arrowsmith,A.Edwards,A.Bochkarev,S.Dhe- Paganon,Structural Genomics Consortium (Sgc)
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Key ref:
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D.R.Littler
et al.
(2006).
Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.
Biochem Biophys Res Commun,
349,
1182-1189.
PubMed id:
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Date:
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04-Jan-06
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Release date:
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17-Jan-06
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PROCHECK
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Headers
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References
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P24723
(KPCL_HUMAN) -
Protein kinase C eta type from Homo sapiens
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Seq:
Struc:
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683 a.a.
140 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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Enzyme class:
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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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Biochem Biophys Res Commun
349:1182-1189
(2006)
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PubMed id:
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Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.
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D.R.Littler,
J.R.Walker,
Y.M.She,
P.J.Finerty,
E.M.Newman,
S.Dhe-Paganon.
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ABSTRACT
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Protein kinase C eta (PKCeta) is one of several PKC isoforms found in humans. It
is a novel PKC isoform in that it is activated by diacylglycerol and anionic
phospholipids but not calcium. The crystal structure of the PKCeta-C2 domain,
which is thought to mediate anionic phospholipid sensing in the protein, was
determined at 1.75 A resolution. The structure is similar to that of the PKC
epsilon C2 domain but with significant variations at the putative lipid-binding
site. Two serine residues within PKC eta were identified in vitro as potential
autophosphorylation sites. In the unphosphorylated structure both serines line
the putative lipid-binding site and may therefore play a role in the
lipid-regulation of the kinase.
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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.A.Leonard,
B.Różycki,
L.F.Saidi,
G.Hummer,
and
J.H.Hurley
(2011).
Crystal structure and allosteric activation of protein kinase C βII.
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Cell,
144,
55-66.
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PDB code:
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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
code is
shown on the right.
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Links
