Diacylglycerol kinase
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
== Function == | == Function == | ||
| - | '''Diacylglycerol kinase''' (DAGK) catalyzes the conversion of diacylglycerol to phosphaditic acid using ATP as energy source. DAGK is active upon receptor activation of the phosphoinositide pathway.<ref>PMID:18062770</ref> | + | '''Diacylglycerol kinase''' (DAGK) catalyzes the conversion of diacylglycerol to phosphaditic acid using ATP as energy source. DAGK is active upon receptor activation of the phosphoinositide pathway.<ref>PMID:18062770</ref> The bacterial DAGK contains 2 families: DgkA and DgkB. |
| - | + | ||
| - | + | ||
== Relevance == | == Relevance == | ||
| + | |||
| + | DAGK is tested as a possible therapeutic target for neuronal diseases. | ||
== Structural highlights == | == Structural highlights == | ||
| - | In DAGK | + | In DAGK DgkB the nucleotide binding site is found at the interface between the 2 domains of the structure.<ref>PMID:18611377</ref> |
</StructureSection> | </StructureSection> | ||
| Line 19: | Line 19: | ||
{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *Diacylglycerol kinase | + | *Diacylglycerol kinase DgkA |
**[[3ze4]], [[4up6]] – EcDAGK – ''Escherichia coli'' <br /> | **[[3ze4]], [[4up6]] – EcDAGK – ''Escherichia coli'' <br /> | ||
| Line 30: | Line 30: | ||
**[[1r79]] – hDAGK delta1 C1 domain - NMR<br /> | **[[1r79]] – hDAGK delta1 C1 domain - NMR<br /> | ||
| - | *Diacylglycerol kinase | + | *Diacylglycerol kinase DgkB |
| - | **[[2qvl]] – | + | **[[2qvl]] – DgkB – ''Staphylococcus aureus''<br /> |
| - | **[[2qv7]] – | + | **[[2qv7]] – DgkB + ADP<br /> |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:35, 24 December 2015
| |||||||||||
3D Structures of diacylglycerol kinase
Updated on 24-December-2015
References
- ↑ Merida I, Avila-Flores A, Merino E. Diacylglycerol kinases: at the hub of cell signalling. Biochem J. 2008 Jan 1;409(1):1-18. PMID:18062770 doi:http://dx.doi.org/10.1042/BJ20071040
- ↑ Miller DJ, Jerga A, Rock CO, White SW. Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases. Structure. 2008 Jul;16(7):1036-46. PMID:18611377 doi:http://dx.doi.org/10.1016/j.str.2008.03.019
