Fig. 2 | Nature Communications

Fig. 2

From: Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association

Fig. 2

The unique features of SgK223 PsK domain. a Interaction between N-lobe of the PsK domain and the dimerization domain. b Interaction between the C-lobe of the PsK domain and the dimerization domain. αN1, cyan; PsK domain, grey; αJ, salmon; αK violet; αL yellow; A-loop, green; C-loop, yellow; αC is modelled in blue dashed lines. c Comparison of the nucleotide binding site of PKA (left) and SgK223 (right). PKA, salmon; ATP, black; SgK223, grey, residues occupying the ATP-binding sites shown in red. d Location of C- and R-spines on PKA and SgK223. C-spine, yellow; R-spine, green; αF, dark red

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