Primate protein-ligand interfaces exhibit significant conservation and unveil human-specific evolutionary drivers.

ABSTRACT: Despite the vast phenotypic differences observed across primates, their protein products are largely similar to each other at the sequence level. We hypothesized that, since proteins accomplish all their functions via interactions with other molecules, alterations in the sites that participate in these interactions may be of critical importance. To uncover the extent to which these sites evolve across primates, we built a structurally-derived dataset of ~4,200 one-to-one orthologous sequence groups across 18 primate species, consisting of ~68,000 ligand-binding sites that interact with DNA, RNA, small molecules, ions, or peptides. Using this dataset, we identify functionally important patterns of conservation and variation within the amino acid residues that facilitate protein-ligand inter

SUBMITTER: King SB 

PROVIDER: S-EPMC10035887 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature