4nfn | pdb_00004nfn

Human tau tubulin kinase 1 (TTBK1) complexed with 3-({5-[(4-amino-4-methylpiperidin-1-yl)methyl]pyrrolo[2,1-f][1,2,4]triazin-4-yl}amino)-5-bromophenol

spinqualitylabelsall models 4nfn, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nfn is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.42Å Ligands: 2KC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TTBK1_HUMAN Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA