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- Title
Structure and inhibition analysis of the mouse SAD-B C-terminal fragment.
- Authors
Ma, Hui; Wu, Jing-Xiang; Wang, Jue; Wang, Zhi-Xin; Wu, Jia-Wei
- 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. The crystal structure and inhibition analysis of the SAD-B AIS-KA1 fragment.
- Subjects
CYCLIC-AMP-dependent protein kinase; CRYSTAL structure; C-terminal binding proteins
- Publication
Bioscience, Biotechnology & Biochemistry, 2016, Vol 80, Issue 10, p1939
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2016.1191331