Journal: Cancers

Article Title: Mutation in the Common Docking Domain Affects MAP Kinase ERK2 Catalysis and Stability

doi: 10.3390/cancers15112938

Figure Lengend Snippet: The human phosphorylated-ERK2 (P-ERK2) D321N (in red) bound to inhibitor AZD0364 (in cyan). In green, the activation loop that begins with the sequence DFG and ends with the sequence APE. The dotted line underlines the undefined region of the three TEY amino acids, important for the activation of ERK2. In cyan, the compound AZD0364 that binds in two opposite regions the mutant D321N.

Article Snippet: The variant was incubated with 1 mM AZD0364 (Cayman Item No. 29827) and crystallized using the reservoir solutions containing 1.6 M MgSO 4 and 0.1 M MES, pH 6.0.

Techniques: Activation Assay, Sequencing, Mutagenesis

Journal: Cancers

Article Title: Mutation in the Common Docking Domain Affects MAP Kinase ERK2 Catalysis and Stability

doi: 10.3390/cancers15112938

Figure Lengend Snippet: Structural comparison of the human phosphorylated-ERK2 (P-ERK2) D321N bound to inhibitor AZD0364 (in cyan). Superposition of the human P-ERK2 D321N (in red), rat P-ERK2 wild-type (in yellow, pdb: 2erk), and rat NP-ERK2 D321N (in gray, pdb: 6ot6). The residues T185 and Y187, important for the activation of ERK2, are depicted in sticks. The dotted line underlines the undefined region of the three TEY amino acids involved in ERK2 activation.

Article Snippet: The variant was incubated with 1 mM AZD0364 (Cayman Item No. 29827) and crystallized using the reservoir solutions containing 1.6 M MgSO 4 and 0.1 M MES, pH 6.0.

Techniques: Comparison, Activation Assay