The structure of Ribonuclease A (RNase A) comprises of four disulfide and catalytic triad of two histidines crucial for its functionality.
[2] RNase A displays three-dimensional domain swapping of the α-helical N-terminal and the C-terminal β-strand. It can exist as dimer or oligomers.
[8] The level of RNase is elevated in cancers and infectious diseases.
[9] RNase A family of enzymes serve as potential drug targets.
[2] The homolog and variants of RNase A are potential chemotherapeutic agents.
[10]