Abstract

Proteins are composed of functional units and carry out their functions primarily through their constituent domains which are the independent folding groups. In this study, we explore the structure-function relationships among therapeutic proteins. We collected sequence data of the therapeutic proteins from Drug Bank and KEGG databases, then grouped different mechanistic and therapeutic classes. Each group was labeled based on structural functional groups in pharmaceutical applications by CATH database tool. This was performed by the domain information, functional families (Fun Fams), evolution, and the structural diversity of a superfamily, which is presented in CATH. Eight classes could be made for the various functionalities, and a corresponding correlation between each class and the relevant structure of the therapeutic protein category using RMSD scores was built. The most frequent functions were cytokine and protease activity that can be achieved by diverse folds of domains. These findings, not only help the structural biologist design better drugs but also clarify the structure-function relationship in those groups.