Biophysical and x-ray crystallographic analysis of Mps1 kinase inhibitor complexes

Biophysical and structural studies of protein kinase monopolar spindle 1 (Mps1) catalytic domain was carried out in the presence of ATP and the aspecific model kinase inhibitor staurosporine to understand the nucleotide binding site architecture of Mps1. The results for the structure of the Mps1 ATP-binding site provide new biophysical insights into Mps1-ligand interactions that would be useful for the design of specific Mps1 inhibitors, including those employing a therapeutically validated quinazoline template.