4NFM
Human tau tubulin kinase 1 (TTBK1)
Summary for 4NFM
| Entry DOI | 10.2210/pdb4nfm/pdb |
| Related | 4NFN |
| Descriptor | Tau-tubulin kinase 1, GLYCEROL (3 entities in total) |
| Functional Keywords | protein kinase, phosphotransferase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q5TCY1 |
| Total number of polymer chains | 1 |
| Total formula weight | 37975.67 |
| Authors | Sheriff, S. (deposition date: 2013-10-31, release date: 2014-02-05, Last modification date: 2023-09-20) |
| Primary citation | 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. 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, 70:173-181, 2014 Cited by 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. PubMed: 24637750DOI: 10.1107/S2053230X14000144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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