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The structure of human tau‐tubulin kinase 1 both in the apo form and in complex with an inhibitor
Author(s) -
Kiefer Susan E.,
Chang ChiehYing J.,
Kimura S. Roy,
Gao Mian,
Xie Dianlin,
Zhang Yaqun,
Zhang Guifen,
Gill Martin B.,
Mastalerz Harold,
Thompson Lorin A.,
Cacace Angela M.,
Sheriff Steven
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14000144
Subject(s) - casein kinase 2 , cyclin dependent kinase 9 , map2k7 , mitogen activated protein kinase kinase , map kinase kinase kinase , kinase , cyclin dependent kinase 2 , casein kinase 2, alpha 1 , protein kinase domain , ask1 , biology , microbiology and biotechnology , biochemistry , chemistry , protein kinase a , gene , mutant
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.