5IRI

Structure of the mouse SAD-B AIS-KA1 fragment

Summary for 5IRI

• Entry DOI: 10.2210/pdb5iri/pdb
• Descriptor: Serine/threonine-protein kinase BRSK1 (2 entities in total)
• Functional Keywords: auto-inhibition, kinase associate-1 domain, transferase
• Biological source: Mus musculus (Mouse)
• Cellular location: Cytoplasm : Q5RJI5
• Total number of polymer chains: 2
• Total formula weight: 30696.62

Authors

Ma, H.,Wu, J.X.,Wang, J.,Wu, J.W. (deposition date: 2016-03-13, release date: 2016-06-15, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)