When is a lipid kinase not a lipid kinase? When it is a protein kinase
Article Abstract:
Some phosphatidylinositol 3-kinases (Pl 3-kinases), which are protein-tyrosine kinases, have both lipid kinase and protein kinase activity, indicating complex behavior of these chemicals. The Pl 3-kinase families are also involved in DNA repair and damage response. A catalytic domain of Pl 3-kinase, p110, has a related Mn2+ -dependent protein kinase activity and phosphorylates Ser-608, in the p85 subunit. This suppresses Pl 3-kinase activity. A conventional protein kinase catalytic domain is absent in the large catalytic subunit of a double-stranded DNA-dependent protein kinase but it has a Pl 3-kinase domain.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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CaMKll structure-An elegant design
Article Abstract:
CaMKll, a protein kinase important in the cellular response to changes in intracellular calcium ion concentration plays a major mediator of calcium signaling in the brain, heart and other tissues, which in term plays a key role in learning and memory. Using a crystal structure of protein kinases some of the biomedical properties of this enzyme CaMKll can be understood.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
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Structure of the autoinhibited kinase domain of CaMKll and SAXS analysis of the holoenzyme
Article Abstract:
Protein kinase-ll (CaMKll) is unique among protein kinases for its dodecameric assembly and its complex responses to Ca(super 2+). Data of the holoenzyme indicates that inactive CaMKll forms tightly packed autoinhibited assemblies that convert when activated form clusters of independent kinase domains.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
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