Abstract
Quercetin, a prevalent plant flavonoid, demonstrates many biological functions through its interaction with distinct protein targets. Recent structural investigations of protein-quercetin complexes have elucidated the molecular mechanism behind these actions. This paper presents a thorough structural analysis of experimentally established protein-quercetin complex structures published to date. The structure of the protein-quercetin complex elucidates the molecular mechanism by which quercetin influences protein function. These structures illustrate how quercetin's chemical characteristics facilitate diverse modes of action by enabling particular interactions with the target protein. This structural knowledge provides the molecular foundation for comprehending quercetin's biological roles and indicates avenues for future structural investigations of flavonoid-protein complexes, especially those with ambiguous molecular processes.