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Nov 11, 2019 · The identification and clarification of the mechanisms of action of drugs used against leishmaniasis may improve their administration ...
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Although a typical two-domain serine/threonine protein kinase fold is observed, the inter-domain hinge region is unusual in both sequence and conformation ...
This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include catalytic domain of dual ...
Missing: Fold| | Show results with:Fold|
In vitro analyses show that the kinase domain of AKT1 physically interacts with the N-terminus (residues 1–446) of DNMT1.52 Importantly, blocking the activity ...
Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition ...
In terms of its catalytic role, the kinase domain has three functions: the binding of the ATP (or GTP) phosphate donor as a complex with a divalent cation ( ...
Serine Threonine-Protein Kinase|Atp-Recognition|Kinase-Inhibitor Complex|Rubredoxin Fold|Tpr Domain|Transferase from en.m.wikipedia.org
A serine/threonine protein kinase (EC 2.7.11.-) is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid ...
Missing: Fold| | Show results with:Fold|
Regarded as constitutively active enzymes, known to participate in many, diverse biological processes, the intracellular regulation bestowed on the CK1.
Serine/threonine-protein kinases; Tyrosine-protein kinases; Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins).
Mar 4, 2012 · STK25 pays a role in determining the proper localisation and morphology of the Golgi complex: inhibition of STK25 function by RNA interference ...