5IRI

Structure of the mouse SAD-B AIS-KA1 fragment

5IRI の概要

• エントリーDOI: 10.2210/pdb5iri/pdb
• 分子名称: Serine/threonine-protein kinase BRSK1 (2 entities in total)
• 機能のキーワード: auto-inhibition, kinase associate-1 domain, transferase
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cytoplasm : Q5RJI5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30696.62

構造登録者

Ma, H.,Wu, J.X.,Wang, J.,Wu, J.W. (登録日: 2016-03-13, 公開日: 2016-06-15, 最終更新日: 2023-11-08)

主引用文献

Ma, H.,Wu, J.X.,Wang, J.,Wang, Z.X.,Wu, J.W.
Structure and inhibition analysis of the mouse SAD-B C-terminal fragment
Biosci.Biotechnol.Biochem., 2016

PubMed Abstract: The SAD (synapses of amphids defective) kinases, including SAD-A and SAD-B, play important roles in the regulation of neuronal development, cell cycle, and energy metabolism. Our recent study of mouse SAD-A identified a unique autoinhibitory sequence (AIS), which binds at the junction of the kinase domain (KD) and the ubiquitin-associated (UBA) domain and exerts autoregulation in cooperation with UBA. Here, we report the crystal structure of the mouse SAD-B C-terminal fragment including the AIS and the kinase-associated domain 1 (KA1) at 2.8 Å resolution. The KA1 domain is structurally conserved, while the isolated AIS sequence is highly flexible and solvent-accessible. Our biochemical studies indicated that the SAD-B AIS exerts the same autoinhibitory role as that in SAD-A. We believe that the flexible isolated AIS sequence is readily available for interaction with KD-UBA and thus inhibits SAD-B activity.

PubMed: 27251228
DOI: 10.1080/09168451.2016.1191331

実験手法

X-RAY DIFFRACTION (2.8 Å)