1U5Q

Crystal Structure of the TAO2 Kinase Domain: Activation and Specifity of a Ste20p MAP3K

1U5Q の概要

• エントリーDOI: 10.2210/pdb1u5q/pdb
• 関連するPDBエントリー: 1U5R
• 分子名称: serine/threonine protein kinase TAO2, CALCIUM ION (3 entities in total)
• 機能のキーワード: serine/threonine protein kinase, transferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasmic vesicle membrane; Multi-pass membrane protein (By similarity). Isoform 2: Cell projection, dendrite: Q9JLS3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79901.09

構造登録者

Zhou, T.,Raman, M.,Gao, Y.,Earnest, S.,Chen, Z.,Machius, M.,Cobb, M.H.,Goldsmith, E.J. (登録日: 2004-07-28, 公開日: 2004-10-12, 最終更新日: 2024-10-30)

主引用文献

Zhou, T.,Raman, M.,Gao, Y.,Earnest, S.,Chen, Z.,Machius, M.,Cobb, M.H.,Goldsmith, E.J.
Crystal Structure of the TAO2 Kinase Domain; Activation and Specificity of a Ste20p MAP3K.
STRUCTURE, 12:1891-1900, 2004

PubMed Abstract: TAO2 is a mitogen-activated protein kinase kinase kinase (MAP3K) that doubly phosphorylates and activates the MAP kinase kinases (MAP2Ks) MEK3 and MEK6. The structure of the kinase domain of TAO2 (1-320) has been solved in its phosphorylated active conformation. The structure, together with structure-based mutagenic analysis, reveals that positively charged residues in the substrate binding groove mediate the first step in the dual phosphorylation of MEK6, on the threonine residue in the motif DS*VAKT*I (*denotes phosphorylation site) of MEK6. TAO2 is a Ste20p homolog, and the structure of active TAO2, in comparison with that of low-activity p21-activated protein kinase (PAK1), a Ste20p-related MAP4K, reveals how this group of kinases is activated by phosphorylation. Finally, active TAO2 displays unusual interactions with ATP, involving, in part, a subgroup-specific C-terminal extension of TAO2. The observed interactions may be useful in making specific inhibitors of TAO kinases.

PubMed: 15458637
DOI: 10.1016/j.str.2004.07.021

実験手法

X-RAY DIFFRACTION (2.1 Å)