Structural optimization for pyrimidine analogues inhibitors against MAP kinase interacting serine/threonine kinase 1(MNK1) based on molecular simulation

2021 ◽  
pp. 130688
Author(s):  
Guangping Li ◽  
Le Fu ◽  
Qingxiu He ◽  
Yong Hu ◽  
Xianlong Su ◽  
...  
Keyword(s):  
Structural Optimization ◽  
Map Kinase ◽  
Molecular Simulation ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Pyrimidine Analogues

scholarly journals Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation

1991 ◽  
Vol 19 (13) ◽  
pp. 3743-3743 ◽  
Author(s):  
Jeng-Horng Her ◽  
Jie Wu ◽  
Thomas B. Rall ◽  
Thomas W. Sturgill ◽  
Michael J. Weber
Keyword(s):  
Map Kinase ◽  
Tyrosine Phosphorylation ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Kinase A

Beneficial effects of IL-1 cytokine inactivation and the role of the serine/threonine kinase MK-2 in hepatic steatosis in a murine obesity model

2015 ◽  
Vol 53 (12) ◽  
Author(s):  
J Wohlfahrt ◽  
A Fettelschoss ◽  
T Kündig ◽  
H Hermanns ◽  
B Müllhaupt ◽  
...  
Keyword(s):  
Hepatic Steatosis ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Beneficial Effects

Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis

2008 ◽  
Vol 415 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Meghna Thakur ◽  
Pradip K. Chakraborti
Keyword(s):  
Protein Kinases ◽  
Solid Phase ◽  
Morphological Changes ◽  
Binding Assays ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Peptidoglycan Biosynthesis ◽  
Vitro Binding ◽  
Solid Phase Binding

Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.

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