Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein

Michiko Kitano-Takahashi; Hiroyuki Morita; Shin Kondo; Kayoko Tomizawa; Ryohei Kato; Michikazu Tanio; Yoshiko Shirota; Hiroshi Takahashi; Shigetoshi Sugio; Toshiyuki Kohno

doi:10.1107/S1744309107028783

Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein

Michiko Kitano-Takahashi, Hiroyuki Morita, Shin Kondo, Kayoko Tomizawa, Ryohei Kato, Michikazu Tanio, Yoshiko Shirota, Hiroshi Takahashi, Shigetoshi Sugio^*, Toshiyuki Kohno

^*この論文の責任著者

和漢医薬学総合研究所研究開発部門資源開発分野（天然物創薬学領域）

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

21 被引用数 (Scopus)

抄録

Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. Functional analyses revealed that a recombinant kinase domain (residues 1-331) of human TTBK2 expressed in insect cells with a baculovirus overexpression system retains kinase activity for tau protein. The kinase domain of TTBK2 was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P2₁2₁2₁, with unit-cell parameters a = 55.6, b = 113.7, c = 117.3 Å, α = β = γ = 90.0°. Diffraction data were collected to 2.9 Å resolution using synchrotron radiation at BL24XU of SPring-8.

本文言語	英語
ページ（範囲）	602-604
ページ数	3
ジャーナル	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
巻	63
号	7
DOI	https://doi.org/10.1107/S1744309107028783
出版ステータス	出版済み - 2007/06/15

ASJC Scopus 主題領域

生物理学
構造生物学
生化学
遺伝学
凝縮系物理学

文献へのアクセス

10.1107/S1744309107028783

引用スタイル

Kitano-Takahashi, M., Morita, H., Kondo, S., Tomizawa, K., Kato, R., Tanio, M., Shirota, Y., Takahashi, H., Sugio, S., & Kohno, T. (2007). Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(7), 602-604. https://doi.org/10.1107/S1744309107028783

@article{1caa5c500bd6475f8ac5a39446001ef3,

title = "Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein",

abstract = "Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. Functional analyses revealed that a recombinant kinase domain (residues 1-331) of human TTBK2 expressed in insect cells with a baculovirus overexpression system retains kinase activity for tau protein. The kinase domain of TTBK2 was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P212121, with unit-cell parameters a = 55.6, b = 113.7, c = 117.3 {\AA}, α = β = γ = 90.0°. Diffraction data were collected to 2.9 {\AA} resolution using synchrotron radiation at BL24XU of SPring-8.",

keywords = "Tau protein, Tau-tubulin kinase",

author = "Michiko Kitano-Takahashi and Hiroyuki Morita and Shin Kondo and Kayoko Tomizawa and Ryohei Kato and Michikazu Tanio and Yoshiko Shirota and Hiroshi Takahashi and Shigetoshi Sugio and Toshiyuki Kohno",

year = "2007",

month = jun,

day = "15",

doi = "10.1107/S1744309107028783",

language = "英語",

volume = "63",

pages = "602--604",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "7",

}

Kitano-Takahashi, M, Morita, H, Kondo, S, Tomizawa, K, Kato, R, Tanio, M, Shirota, Y, Takahashi, H, Sugio, S & Kohno, T 2007, 'Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 7, pp. 602-604. https://doi.org/10.1107/S1744309107028783

Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein. / Kitano-Takahashi, Michiko; Morita, Hiroyuki; Kondo, Shin その他.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 7, 15.06.2007, p. 602-604.

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

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AU - Kitano-Takahashi, Michiko

AU - Morita, Hiroyuki

AU - Kondo, Shin

AU - Tomizawa, Kayoko

AU - Kato, Ryohei

AU - Tanio, Michikazu

AU - Shirota, Yoshiko

AU - Takahashi, Hiroshi

AU - Sugio, Shigetoshi

AU - Kohno, Toshiyuki

PY - 2007/6/15

Y1 - 2007/6/15

N2 - Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. Functional analyses revealed that a recombinant kinase domain (residues 1-331) of human TTBK2 expressed in insect cells with a baculovirus overexpression system retains kinase activity for tau protein. The kinase domain of TTBK2 was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P212121, with unit-cell parameters a = 55.6, b = 113.7, c = 117.3 Å, α = β = γ = 90.0°. Diffraction data were collected to 2.9 Å resolution using synchrotron radiation at BL24XU of SPring-8.

AB - Tau-tubulin kinase 2 (TTBK2) is a Ser/Thr kinase that putatively phosphorylates residues Ser208 and Ser210 (numbered according to a 441-residue human tau isoform) in tau protein. Functional analyses revealed that a recombinant kinase domain (residues 1-331) of human TTBK2 expressed in insect cells with a baculovirus overexpression system retains kinase activity for tau protein. The kinase domain of TTBK2 was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P212121, with unit-cell parameters a = 55.6, b = 113.7, c = 117.3 Å, α = β = γ = 90.0°. Diffraction data were collected to 2.9 Å resolution using synchrotron radiation at BL24XU of SPring-8.

KW - Tau protein

KW - Tau-tubulin kinase

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Expression, purification and crystallization of a human tau-tubulin kinase 2 that phosphorylates tau protein

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