PDBsum entry 4nfm

Transferase

PDB id: 4nfm

Contents

Protein chain

293 a.a.

Ligands

GOL

Waters ×80

PDB id:

4nfm

Name:

Transferase

Title:

Human tau tubulin kinase 1 (ttbk1)

Structure:

Tau-tubulin kinase 1. Chain: a. Fragment: kinase domain (unp residues 13-343). Synonym: brain-derived tau kinase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ttbk1, bdtk, kiaa1855. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

2.12Å R-factor: 0.206 R-free: 0.241

Authors:

S.Sheriff

Key ref:

S.E.Kiefer et al. (2014). 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. PubMed id: 24637750 DOI: 10.1107/S2053230X14000144

Date:

31-Oct-13 Release date: 05-Feb-14

Protein chain

Q5TCY1  (TTBK1_HUMAN) -  Tau-tubulin kinase 1 from Homo sapiens

Seq: 1321 a.a.

Struc: 293 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S2053230X14000144

Acta Crystallogr F Struct Biol Commun 70:173-181 (2014)

PubMed id: 24637750

The structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitor.

S.E.Kiefer, C.J.Chang, S.R.Kimura, M.Gao, D.Xie, Y.Zhang, G.Zhang, M.B.Gill, H.Mastalerz, L.A.Thompson, A.M.Cacace, S.Sheriff.

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.