Figure 4 | Scientific Reports

Figure 4

From: Activation of RSK by phosphomimetic substitution in the activation loop is prevented by structural constraints

Figure 4The alternative text for this image may have been generated using AI.

Molecular dynamics simulation of RSK2 in the active and phosphomimetic forms. (A) The RMSD time traces during the MD simulation show a rapid increase within 2 ns. Then, pSer227 simulation shows a slow increase in the RMSD, while Asp227 simulation presents a plateau. (B) The RMSF profiles show that αC-helix (residues from 119 to 124) and the DFG region (from 221 to 218) were more flexible in the mutant RSK2 S227D than in the active wild type protein (pSer227). (C) The crystal structures of the activation loop of phosphorylated wild type RSK2 and of (D) the phosphomimetic form obtained after MD simulation of PDB ID 4NW5. pSer227 after MD simulation maintains all the three bonds shown in the crystal structure with Arg114, Lys216 and Arg192. On the contrary, Asp227 in the phosphomimetic protein interacts only with Lys216 and Arg192.

Back to article page