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. Author manuscript; available in PMC: 2023 Jan 3.
Published in final edited form as: Biochemistry. 2022 Sep 7;61(18):1955–1965. doi: 10.1021/acs.biochem.2c00378

Figure 6.

Figure 6.

Comparison of CaM/CaM1 vs CaM/CNGA2 and CaM/CaM2 vs CaM/CK. Main chain structures of (A) CaM/CaM1 (PDB ID: 8DGK), (B) CaM/CNGA2 (PDB ID: 1SY9), (D) CaM/CaM2 (PDB ID: 8DGH), and (E) CaM/CK (PDB ID: 7BF2). Main chain structures of CaM/CaM1 overlaid with CaM/CNGA2 (C) and CaM/CaM2 overlaid with CaM/CK (F). The CaM N-lobe (cyan) is bound to CaM1 (magenta helix) in panels A and C; the CaM N-lobe (green) is bound to CNGA2 (blue helix) in panels B and C; the CaM C-lobe (dark cyan) is bound to CaM2 (light red helix) in panels D and F; the CaM C-lobe (yellow) is bound to the peptide fragment of the creatine kinase (CK, purple helix) in panels E and F.