scholarly journals Deciphering the Structural Basis of Eukaryotic Protein Kinase Regulation

PLoS Biology ◽  
2013 ◽  
Vol 11 (10) ◽  
pp. e1001680 ◽  
Author(s):  
Hiruy S. Meharena ◽  
Philip Chang ◽  
Malik M. Keshwani ◽  
Krishnadev Oruganty ◽  
Aishwarya K. Nene ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Structural Basis ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein ◽  
Kinase Regulation

The Eukaryotic Protein Kinase Domain

2005 ◽  
pp. 181-209 ◽  
Author(s):  
Arvin C. Dar ◽  
Leanne E. Wybenga-Groot ◽  
Frank Sicheri
Keyword(s):  
Protein Kinase ◽  
Kinase Domain ◽  
Protein Kinase Domain ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein

scholarly journals Assignment of Backbone Resonances in a Eukaryotic Protein Kinase – ERK2 as a Representative Example

2011 ◽  
pp. 359-368 ◽  
Author(s):  
Andrea Piserchio ◽  
Kevin N. Dalby ◽  
Ranajeet Ghose
Keyword(s):  
Protein Kinase ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein

scholarly journals Screening of Microbial Extracts for Anticancer Compounds Using Streptomyces Kinase Inhibitor Assay

2015 ◽  
Vol 10 (7) ◽  
pp. 1934578X1501000 ◽  
Author(s):  
Prashant Shanbhag ◽  
Sarita Bhave ◽  
Ashwini Vartak ◽  
Asha Kulkarni-Almeida ◽  
Girish Mahajan ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Anticancer Agents ◽  
Kinase Inhibitors ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitors ◽  
Kinase Assay ◽  
Diffusion Method ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein ◽  
Microbial Extracts

Eukaryotic kinases are known to play an important role in signal transduction pathways by phosphorylating their respective substrates. Abnormal phosphorylations by these kinases have resulted in diseases. Hence inhibitors of kinases are of considerable pharmaceutical interest for a wide variety of disease targets, especially cancers. A number of reports have been published which indicate that eukaryotic-like kinases may complement two-component kinase systems in several bacteria. In Streptomyces sp. such kinases have been found to have a role in formation of aerial hyphae, spores, pigmentation & even in antibiotic production in some strains. Eukaryotic kinase inhibitors are seen to inhibit formation of aerial mycelia in Streptomyces without inhibiting vegetative mycelia. This property has been used to design an assay to screen for eukaryotic kinase inhibitors. The assay involves testing of compounds against Streptomyces 85E ATCC 55824 using agar well diffusion method. Inhibitors of kinases give rise to “bald” colonies where aerial mycelia and sporulation inhibition is seen. The assay has been standardized using known eukaryotic protein kinase inhibiting anticancer agents like AG-490, AG-1295, AG-1478, Flavopiridol and Imatinib as positive controls, at a concentration ranging from 10 μg/well to 100 μg/well. Anti-infective compounds which are not reported to inhibit eukaryotic protein kinases were used as negative controls. A number of microbial cultures have been screened for novel eukaryotic protein kinase inhibitors. Further these microbial extracts were tested in various cancer cell lines like Panc1, HCT116, Calu1, ACHN and H460 at a concentration of 10 μg/mL/ well. The anticancer data was seen correlating well with the Streptomyces kinase assay thus validating the assay.

scholarly journals Purification of two Bacillus subtilis proteins which cross-react with antibodies directed against eukaryotic protein kinase C, the His HPr kinase and trigger factor

Microbiology ◽  
1997 ◽  
Vol 143 (4) ◽  
pp. 1151-1161 ◽  
Author(s):  
N. Zouari ◽  
B. Roche ◽  
J. F. M. L. Seegers ◽  
S. J. Seror
Keyword(s):  
Bacillus Subtilis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Trigger Factor ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein ◽  
Kinase C

scholarly journals A Conserved Glu–Arg Salt Bridge Connects Coevolved Motifs That Define the Eukaryotic Protein Kinase Fold

2012 ◽  
Vol 415 (4) ◽  
pp. 666-679 ◽  
Author(s):  
Jie Yang ◽  
Jian Wu ◽  
Jon M. Steichen ◽  
Alexandr P. Kornev ◽  
Michael S. Deal ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Salt Bridge ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein

scholarly journals Kinannote, a computer program to identify and classify members of the eukaryotic protein kinase superfamily

2013 ◽  
Vol 29 (19) ◽  
pp. 2387-2394 ◽  
Author(s):  
Jonathan M. Goldberg ◽  
Allison D. Griggs ◽  
Janet L. Smith ◽  
Brian J. Haas ◽  
Jennifer R. Wortman ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Computer Program ◽  
Eukaryotic Protein Kinase ◽  
Eukaryotic Protein

scholarly journals Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Michael R. Oliver ◽  
Christopher R. Horne ◽  
Safal Shrestha ◽  
Jeremy R. Keown ◽  
Lung-Yu Liang ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Regulatory Protein ◽  
Active Conformation ◽  
Eukaryotic Protein Kinase ◽  
Agc Kinases ◽  
Eukaryotic Protein ◽  
Parallel Side ◽  
Viral Protein Kinase ◽  
Catalytically Active ◽  
Β Sheet

AbstractThe life cycle of Baculoviridae family insect viruses depends on the viral protein kinase, PK-1, to phosphorylate the regulatory protein, p6.9, to induce baculoviral genome release. Here, we report the crystal structure of Cydia pomenella granulovirus PK-1, which, owing to its likely ancestral origin among host cell AGC kinases, exhibits a eukaryotic protein kinase fold. PK-1 occurs as a rigid dimer, where an antiparallel arrangement of the αC helices at the dimer core stabilizes PK-1 in a closed, active conformation. Dimerization is facilitated by C-lobe:C-lobe and N-lobe:N-lobe interactions between protomers, including the domain-swapping of an N-terminal helix that crowns a contiguous β-sheet formed by the two N-lobes. PK-1 retains a dimeric conformation in solution, which is crucial for catalytic activity. Our studies raise the prospect that parallel, side-to-side dimeric arrangements that lock kinase domains in a catalytically-active conformation could function more broadly as a regulatory mechanism among eukaryotic protein kinases.

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