The structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitor.
Kiefer, S.E., Chang, C.J., Kimura, S.R., Gao, M., Xie, D., Zhang, Y., Zhang, G., Gill, M.B., Mastalerz, H., Thompson, L.A., Cacace, A.M., Sheriff, S.(2014) Acta Crystallogr Sect F Struct Biol Cryst Commun 70: 173-181
- PubMed: 24637750 
- DOI: https://doi.org/10.1107/S2053230X14000144
- Primary Citation of Related Structures:  
4NFM, 4NFN - PubMed Abstract: 
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.
Organizational Affiliation: 
Molecular Discovery Technologies, Bristol-Myers Squibb Research and Development, PO Box 4000, Princeton, NJ 08543-4000, USA.