| First Author | Ma H | Year | 2016 |
| Journal | Biosci Biotechnol Biochem | Volume | 80 |
| Issue | 10 | Pages | 1939-46 |
| PubMed ID | 27251228 | Mgi Jnum | J:325964 |
| Mgi Id | MGI:6880801 | Doi | 10.1080/09168451.2016.1191331 |
| Citation | Ma H, et al. (2016) Structure and inhibition analysis of the mouse SAD-B C-terminal fragment. Biosci Biotechnol Biochem 80(10):1939-46 |
| abstractText | 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 A 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. |
