Structural highlights
Function
TTBK1_HUMAN Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU.[1]
Publication Abstract from PubMed
Tau-tubulin kinase 1 (TTBK1) is a dual-specificity (serine/threonine and tyrosine) kinase belonging to the casein kinase 1 superfamily. TTBK1 is a neuron-specific kinase that regulates tau phosphorylation. Hyperphosphorylation of tau is implicated in the pathogenesis of Alzheimer's disease. Two kinase-domain constructs of TTBK1 were expressed in a baculovirus-infected insect-cell system and purified. The purified TTBK1 kinase-domain proteins were crystallized using the hanging-drop vapor-diffusion method. X-ray diffraction data were collected and the structure of TTBK1 was determined by molecular replacement both as an apo structure and in complex with a kinase inhibitor.
The structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitor.,Kiefer SE, Chang CJ, Kimura SR, Gao M, Xie D, Zhang Y, Zhang G, Gill MB, Mastalerz H, Thompson LA, Cacace AM, Sheriff S Acta Crystallogr F Struct Biol Commun. 2014 Feb 1;70(Pt 2):173-81. doi:, 10.1107/S2053230X14000144. Epub 2014 Jan 21. PMID:24637750[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sato S, Cerny RL, Buescher JL, Ikezu T. Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. J Neurochem. 2006 Sep;98(5):1573-84. PMID:16923168 doi:JNC4059
- ↑ Kiefer SE, Chang CJ, Kimura SR, Gao M, Xie D, Zhang Y, Zhang G, Gill MB, Mastalerz H, Thompson LA, Cacace AM, Sheriff S. The structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitor. Acta Crystallogr F Struct Biol Commun. 2014 Feb 1;70(Pt 2):173-81. doi:, 10.1107/S2053230X14000144. Epub 2014 Jan 21. PMID:24637750 doi:http://dx.doi.org/10.1107/S2053230X14000144
