Figure 2: Detailed interactions within the Nek7–Nek9 interface.
From: Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization
(a) Detailed view of the Nek7–Nek9 interaction in the region of Nek9 aa 810–816. (b) Detailed view of the Nek7–Nek9 interaction in the region of Nek9 aa 814–825. (c) Coomassie-stained SDS–PAGE gel showing the results of a GST co-precipitation experiment testing the binding of GST-Nek9-CTD to structure-based mutants of Nek7. (d) Mutagenesis/co-precipitation data from c mapped onto the surface of Nek7. Key binding residues (red), non-essential residues (green) and untested residues (teal).
