BAIT

BRSK1

Gm1100, SAD-B, SADB
BR serine/threonine kinase 1
Mus musculus
PREY

BRSK1

Gm1100, SAD-B, SADB
BR serine/threonine kinase 1
Mus musculus

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structure and inhibition analysis of the mouse SAD-B C-terminal fragment.

Ma H, Wu JX, Wang J, Wang ZX, Wu JW

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, ... [more]

Biosci Biotechnol Biochem Oct. 01, 2016; 80(10);1939-46 [Pubmed: 27251228]

Throughput

  • Low Throughput

Additional Notes

  • Authors state that the dimer observed in our crystal was probably due to crystallization artefacts

Curated By

  • BioGRID