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PDBsum entry 1tbn
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Calcium-binding protein
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PDB id
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1tbn
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References listed in PDB file
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Key reference
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Title
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Nmr structure of a protein kinase c-Gamma phorbol-Binding domain and study of protein-Lipid micelle interactions.
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Authors
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R.X.Xu,
T.Pawelczyk,
T.H.Xia,
S.C.Brown.
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Ref.
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Biochemistry, 1997,
36,
10709-10717.
[DOI no: ]
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PubMed id
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Abstract
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Classical protein kinase C (PKC) family members are activated by the binding of
various ligands to one of several cysteine-rich domains of the enzyme. The
natural agonist, diacylglycerol (DAG), and the natural product superagonist,
phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging
physiological effects. The second cysteine-rich (Cys2) domain of rat brain
PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure
was determined to high resolution using multidimensional heteronuclear NMR
methods. The phorbol binding site was identified by titrating this domain with
phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations
of this domain with lipid micelles, in the absence and presence of phorbols,
indicate selective broadening of some resonances. The observed behavior
indicates conformational exchange between bound and free states upon
protein-micelle interaction. The data also suggest that half of the domain,
including the phorbol site and one of the zinc sites, is capable of inserting
into membranes.
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Secondary reference #1
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Title
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Crystal structure of the cys2 activator-Binding domain of protein kinase c delta in complex with phorbol ester.
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Authors
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G.Zhang,
M.G.Kazanietz,
P.M.Blumberg,
J.H.Hurley.
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Ref.
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Cell, 1995,
81,
917-924.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Solution structure of cysteine-Rich domain of protein kinase c alpha.
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Authors
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S.Ichikawa,
H.Hatanaka,
Y.Takeuchi,
S.Ohno,
F.Inagaki.
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Ref.
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J Biochem (tokyo), 1995,
117,
566-574.
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PubMed id
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Secondary reference #3
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Title
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Solution structure of a cysteine rich domain of rat protein kinase c.
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Authors
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U.Hommel,
M.Zurini,
M.Luyten.
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Ref.
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Nat Struct Biol, 1994,
1,
383-387.
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PubMed id
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