Journal: The Journal of Biological Chemistry
Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures
doi: 10.1074/jbc.M117.783555
Figure Lengend Snippet: Comparison of the Cpd-5 and NMS-P715 bound to C604Y/C604W structures. A, 2mFo − DFc electron density map of Cpd-5 in Mps1 kinase contoured at 1.0σ (carved at 2.5 Å from the Cpd-5 atoms). B, Cpd-5 in the ATP-binding pocket of Mps1 C604Y; Cpd-5, the side chains of Gln541, Tyr604, and Lys553 as well as residue Gly605 are depicted as sticks; hydrogen bonds are depicted as black dotted lines. Figures were made in CCP4mg (38). C, Cpd-5 interactions with Mps1 kinase drawn by the Lidia routine in COOT. D–F, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. G–I, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. J–L, the same as A–C for the interaction of NMS-P715 with Mps1 C604W.
Article Snippet: The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).
Techniques: Comparison, Binding Assay, Residue