The Computational Study of Toxic Heavy Metal Binding to Cancer‐Related Mutation Proteins

Abstract Exposure to nonessential metals causes serious health illnesses such as cancer. The International agency for research on cancer classified arsenic, beryllium, chromium, nickel, and cadmium as group 1 carcinogens. We utilized bioinformatics tools and literature survey methods to identify proteins that bind toxic heavy metals in cancer. In our analysis, 67 toxic heavy metal‐binding proteins are found to act as oncogenes, tumour suppressor genes, and fusion genes. Most proteins bind to lead, indicating that lead likely plays a role in carcinogenesis. Binding site analysis of the proteins reveals that these metals bind in domain regions, including the immunoglobulin‐like domain 2, the protein kinase domain, the WD40 and MH2 repeats, and oligomerization regions. The mutation also affects the protein's structure and function, indicating that a point/missense mutation in its metal‐binding regions has a mostly negative impact on its function and structural stability. This study reveals that binding of heavy toxic metals in protein domains can directly or indirectly inhibit or activate the proteins. Analysing the toxicity of heavy metals in proteins helps determine their role in carcinogenicity.