4YOM

Structure of SAD kinase

4YOM の概要

• エントリーDOI: 10.2210/pdb4yom/pdb
• 関連するPDBエントリー: 4YNZ
• 分子名称: Serine/threonine-protein kinase BRSK2, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: kinase domain, uba domain, ka1 domain, transferase
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : Q69Z98 Q69Z98
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56511.10

構造登録者

Wu, J.X.,Wang, J.,Chen, L.,Wang, Z.X.,Wu, J.W. (登録日: 2015-03-12, 公開日: 2015-12-16, 最終更新日: 2023-11-08)

主引用文献

Wu, J.X.,Cheng, Y.S.,Wang, J.,Chen, L.,Ding, M.,Wu, J.W.
Structural insight into the mechanism of synergistic autoinhibition of SAD kinases
Nat Commun, 6:8953-8953, 2015

PubMed Abstract: The SAD/BRSK kinases participate in various important life processes, including neural development, cell cycle and energy metabolism. Like other members of the AMPK family, SAD contains an N-terminal kinase domain followed by the characteristic UBA and KA1 domains. Here we identify a unique autoinhibitory sequence (AIS) in SAD kinases, which exerts autoregulation in cooperation with UBA. Structural studies of mouse SAD-A revealed that UBA binds to the kinase domain in a distinct mode and, more importantly, AIS nestles specifically into the KD-UBA junction. The cooperative action of AIS and UBA results in an 'αC-out' inactive kinase, which is conserved across species and essential for presynaptic vesicle clustering in C. elegans. In addition, the AIS, along with the KA1 domain, is indispensable for phospholipid binding. Taken together, these data suggest a model for synergistic autoinhibition and membrane activation of SAD kinases.

PubMed: 26626945
DOI: 10.1038/ncomms9953

実験手法

X-RAY DIFFRACTION (2.49 Å)