Discovery of strong inhibitory properties of a monoclonal antibody of PKA and use of the antibody and a competitive photoluminescent orthosteric probe for analysis of the protein kinase.
Adenosine Triphosphate
/ chemistry
Antibodies, Monoclonal
/ chemistry
Antibody Specificity
Binding Sites
Binding, Competitive
Cell Line, Tumor
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
/ analysis
HeLa Cells
Humans
Immunoassay
Kinetics
Luminescent Measurements
Models, Molecular
Molecular Probes
/ chemistry
Peptides
/ chemistry
Phosphorylation
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
ATP-binding pocket
Bisubstrate inhibitor
Inhibitory antibody
Ligand-induced epitope restructuring
Time-gated luminescence
cAMP-dependent protein kinase (PKA)
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
06
12
2019
revised:
01
03
2020
accepted:
07
04
2020
pubmed:
14
4
2020
medline:
22
10
2020
entrez:
14
4
2020
Statut:
ppublish
Résumé
We show that the antibody, clone mAb(D38C6), of the α isoform of the catalytic subunit of PKA (PKAcα) inhibits the kinase-catalyzed phosphorylation with low-nanomolar inhibitory potency (K
Identifiants
pubmed: 32283249
pii: S1570-9639(20)30074-1
doi: 10.1016/j.bbapap.2020.140427
pii:
doi:
Substances chimiques
Antibodies, Monoclonal
0
Molecular Probes
0
Peptides
0
protein kinase inhibitor peptide
128022-93-5
Adenosine Triphosphate
8L70Q75FXE
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
EC 2.7.11.11
protein kinase A Calpha
EC 2.7.11.11
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
140427Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.