2810408P10Rik Inhibitors

Zinc finger protein 933 inhibitors are chemicals that interfere with the proper function or the structural integrity of Zfp933, a member of the zinc finger protein family. Zinc finger domains require coordination with zinc ions to maintain their structure and facilitate their role in DNA, RNA, or protein interactions. Agents such as chelerythrine and clioquinol operate by disrupting these essential interactions. Chelerythrine achieves this by intercalating into DNA and obstructing the access of Zfp933 to its binding sites, while clioquinol chelates the zinc ions, compromising the structural stability of the protein. Disulfiram and Pyrithione Zinc exert their effects by binding to zinc ions, which can result in the distortion of the zinc finger motif, ultimately impairing the protein's function.

Compounds like 1,10-Phenanthroline and TPEN are potent chelators that sequester zinc ions away from the zinc finger domains, leading to a loss of functional conformation. Nitric Oxide Donors introduce nitrosylation reactions that can modify cysteine residues within the zinc finger structures, potentially affecting protein conformation and functionality. Similarly, compounds such as mimosine, NSC 606985, and dithizone bind to metal ions and can, therefore, disturb the interaction between Zfp933 and its essential zinc ions. Ebselen and PDTC can influence the redox state of cysteine residues within zinc finger domains or chelate zinc ions, respectively, both of which can result in altered protein activity.