Supplementary data for PTEN project

The current study set out to investigate the effects of harmful nsSNPs on the stability, functionality, and structure of the PTEN. Eleven mutations were identified as potentially affecting the structural and functional characteristics of the PTEN protein: D107N, G129E, S170R, H123R, C124R, R130G, M35R, L70P, R130Q, L112P, H61D, H93R, D252G, G132V, R173C, R173H, and I135T. All 11 changes happened at highly conserved amino acid residue locations, according to the conservation analysis. Conserved domain analysis predicted the loss of domains in M35R and L70P and the loss of catalytic and active sites in C124R, R130G, and R130Q. In molecular dynamic simulation, it can be observed that mutations R173H and C124R consistently exhibit deviation from wild-type PTEN, indicating greater instability in the structure of the protein. Using a variety of computational tools, the in-silico investigation was carried out to shed light on the role missense mutations play in altering proteins.