Figure 5: Mutations in the Nek7 back-to-back interface.
From: Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization
(a) Structure of autoinhibited Nek7 showing residues involved in the back-to-back interface. (b) Structure of Nek7 in the back-to-back conformation. (c,d) In vitro kinase activity assay of WT Nek7 and Nek7 mutants alone and in the presence of Nek9-CTD. Kinase activity was quantified by scintillation counting. Error bars represent the standard error for two independent reactions. *P<0.05, **P<0.01 and ****P<0.0001 using one-way analysis of variance with Dunnett’s post hoc test compared with the WT reaction for Nek7 alone reactions or to the WT plus N9 CTD reaction for assays performed in the presence of Nek9-CTD.
