Figure 1 | Scientific Reports

Figure 1

From: Met125 is essential for maintaining the structural integrity of calmodulin’s C-terminal domain

Figure 1

Hydrophobic interactions stabilize CaM’s EF hand domains. (a) N- and C-terminal domains of Ca2+-bound (holo) CaM (PDB 1CLL) with Met residues shown in yellow, Phe residues shown in green and the mutation sites 52 and 125 shown in red. (b) Ca2+ binding alters the solvent exposure of CaM’s Met residues (red; PDB 1DMO30 and 1CLL31). For simplicity, residue assignment includes initiator Met. The image was generated using PyMOL Molecular Graphics System, Version 1.832 (https://pymol.org/2/).

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