A Molecular Analysis of the Aminopeptidase P-Related Domain of PID-5 from Caenorhabditis elegans

A novel protein, PID-5, has been shown to be a requirement for germline immortality and recently implicated in RNA-induced epigenetic silencing the Caenorhabditis elegans embryo. Importantly, it contain both an eTudor aminopeptidase P-related domain. However, mechanism not yet fully characterised. In this study, bioinformatic tools were used compare pre-existing P molecular structures AlphaFold2-predicted domain of PID-5 (PID-5 APP-RD). Structural homology, metal composition, inhibitor-bonding interactions, potential dimerisation critically assessed through computational techniques, including structural superimposition protein-ligand docking. Results from research suggest that metallopeptidase-like shares high homology with known enzymes possesses canonical ‘pita-bread fold’. absence conserved metal-coordinating residues indicates only single Zn2+ may bound at active site. The APP-RD form transient interactions inhibitor therefore recognise substrates comparable way structures. loss key catalytic suggests will inactive. Further evidence heterodimerisation C. is feasible predicted regulate proteolytic cleavage pathway. interact PID-2 bring activity Z-granule, where could influence WAGO-4 ensure balanced production 22G-RNA signals transgenerational silencing. Targeted experiments into APPs malaria cancer are required order build upon biological therapeutic significance research.