Catalytic domain crystal structure of protein kinase C-theta (PKCtheta)
pubmed.ncbi.nlm.nih.gov › ...
The structure follows the classic bilobal kinase fold and shows the enzyme in its active conformation and phosphorylated state. Inhibitory interactions between ...
Missing: Transferase
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May 3, 2007 · It is likely that abrogation of inhibitory intramolecular interaction with both the catalytic core and the C2 domain upon PKC activation ...
Here we describe the molecular cloning and deduced primary structure of a cDNA encoding a novel PKC isoform, termed PKC theta, which was isolated in the course ...
gions within the catalytic domain of protein kinases, was used successfully by Mischak et al. (11) to amplify PKC sequences from myeloid cell lines. The ...
The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Protein kinase C theta is an enzyme that in humans is encoded by the PRKCQ gene. PKC-θ, a member of serine/threonine kinases, is mainly expressed in ...
A pseudosubstrate sequence (RRGAIKQA) within the C1a domain of PKC-θ binds to the substrate-binding region in the catalytic domain, inhibiting the PKC-θ kinase ...
Aug 25, 2015 · The signaling output of protein kinase C (PKC) is exquisitely controlled, with its disruption resulting in pathophysiologies.
The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Jan 21, 2005 · This study investigated the molecular mechanisms underlying inhibition of protein kinase C (PKC) ζ by p38 kinase during nitric oxide ...