1ZMV

Catalytic and ubiqutin-associated domains of MARK2/PAR-1: K82R mutant

1ZMV の概要

• エントリーDOI: 10.2210/pdb1zmv/pdb
• 関連するPDBエントリー: 1Y8G 1ZMU 1ZMW
• 分子名称: MAP/Microtubule affinity regulating kinase 2 (1 entity in total)
• 機能のキーワード: serine/threonine protein kinase; mark; par-1; kin1; uba domain, signaling protein, transferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): O08679
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75350.89

構造登録者

Panneerselvam, S.,Marx, A.,Mandelkow, E.-M.,Mandelkow, E. (登録日: 2005-05-11, 公開日: 2006-02-14, 最終更新日: 2023-08-23)

主引用文献

Panneerselvam, S.,Marx, A.,Mandelkow, E.M.,Mandelkow, E.
Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1.
Structure, 14:173-183, 2006

PubMed Abstract: The Ser/Thr kinase MARK2 phosphorylates tau protein at sites that cause detachment from microtubules in Alzheimer neurofibrillary degeneration. Homologs of MARK2 include Par-1 in C. elegans and Drosophila, which generates embryonic polarity. We report the X-ray structure of the catalytic and ubiquitin-associated domains (UBA) of human MARK2. The activity was altered by mutations in the ATP binding site and/or activation loop. The catalytic domain shows the small and large lobes typical of kinases. The substrate cleft is in an inactive, open conformation in the inactivated and the wild-type structure. The UBA domain is attached via a taut linker to the large lobe of the kinase domain and leans against a hydrophobic patch on the small lobe. The UBA structure is unusual because the orientation of its third helix is inverted, relative to previous structures. Possible implications of the structure for the regulation of kinase activity are discussed.

PubMed: 16472737
DOI: 10.1016/j.str.2005.09.022

実験手法

X-RAY DIFFRACTION (3.105 Å)