Extended Data Fig. 4: MD simulations and ITC measurements of the interaction between TRIM7^PRY-SPRY and 2C variants.

a, (left) Structural comparison between TRIM2-2C and the calculated TRIM7-2C (Q329E). (right) Effects of simulations on the Q329E mutation. Molecular dynamics simulation suggested that Q329E mutation eliminates the interactions between the residue 329 and TRIM7, especially the interactions with Arg385, Asn438, and Ser499 in TRIM7 (Supplementary Table 2). Consequently, the C-terminal carboxylate group of 2C at residue 329 is more exposed to solvent, leading to a further reduced TRIM7-2C interaction and increased 2C C-terminal solvation. b, The root-mean-square deviation (RMSD) change of the 2C peptide structures in MD simulation (left). The RMSD values of WT (black) and Q329E (red) 2C peptide structures with reference to the first frame of the trajectory in MD simulation were calculated and plotted. While the WT 2C peptide gradually converged to the original position, the Q329E mutant drifted away as indicated by the increasing RMSD over MD simulation. Right, the Q329E mutation led to increased hydrogen bonding with water. The number of hydrogen-bonded water molecules to the side chain amide of Q329 in WT 2C (black) and the side chain carboxyl of E329 in the mutant (red) were plotted over MD simulation.