Alcohol binding in the C1 (C1A+C1B) domain of protein kinase C epsilon
نویسندگان
چکیده
منابع مشابه
Synthesis and protein kinase C (PKC)-C1 domain binding properties of diacyltetrol based anionic lipids.
The protein kinase C (PKC) family of lipid-activated kinases plays a significant role in the regulation of diverse cellular functions including tumor promotion, apoptosis, differentiation, and others. The lipophilic second messenger diacylglycerols (DAGs) act as endogenous ligands for the PKCs in the presence of anionic phospholipids. To develop effective PKC regulators and understand the impor...
متن کاملConformation of the C1 phorbol-ester-binding domain participates in the activating conformational change of protein kinase C.
The fluorescent phorbol ester 12-N-methylanthraniloylphorbol 13-acetate [sapintoxin D (SAPD)] was used as both the activator and the probe for the activating conformational change of the C1 domain of recombinant protein kinase C (PKC)alpha. Fluorescence emission spectra and steady-state anisotropy measurements of SAPD in fully active membrane-associated PKC show that there is a relatively hydro...
متن کاملAn investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C.
Myosin-binding protein C (MyBP-C) is a myofibril-associated protein found in cardiac and skeletal muscle. The cardiac isoform (cMyBP-C) is subject to reversible phosphorylation and the surface-charge state of the protein is of keen interest with regard to understanding the inter-protein interactions that are implicated in its function. Diffraction data from the C1 domain of cMyBP-C were extende...
متن کاملDevelopment of diacyltetrol lipids as activators for the C1 domain of protein kinase C.
The protein kinase C (PKC) family of serine/threonine kinases is an attractive drug target for the treatment of cancer and other diseases. Diacylglycerol (DAG), phorbol esters and others act as ligands for the C1 domain of PKC isoforms. Inspection of the crystal structure of the PKCδ C1b subdomain in complex with phorbol-13-O-acetate shows that one carbonyl group and two hydroxyl groups play pi...
متن کاملMyofilament anchoring of protein kinase C-epsilon in cardiac myocytes.
Regulatory proteins on muscle filaments are substrates for protein kinase C (PKC) but mechanisms underlying activation and translocation of PKC to this non-membrane compartment are poorly understood. Here we demonstrate that the epsilon isoform of PKC (epsilon-PKC) activated by arachidonic acid (AA) binds reversibly to cardiac myofibrils with an EC(50) of 86 nM. Binding occurred near the Z-line...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - General Subjects
سال: 2015
ISSN: 0304-4165
DOI: 10.1016/j.bbagen.2015.07.005