Structural and functional characterization of protein-metal interactions.

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Metal-binding proteins play crucial roles in regulating a number of biological processes, and there is considerable interest in characterizing the mechanistic details of protein-metal interactions. For example, metals such as calcium, copper, iron and zinc play key biological roles through important protein-metal interactions. In addition to their essential roles, a number of metals are toxic due to their ability to bind proteins in an adverse manner. Toxic metals that pose a serious threat to both our health and environment include mercury, lead, cadmium and arsenic. For the last twenty year, my laboratory has been characterizing the interaction of proteins with both essential and toxic metals. The long-term objectives of our research program are to structurally and functionally characterize the interaction of proteins with both essential and toxic metals. In particular, we are interested in how essential metals help select proteins fold into their functional conformation as well as how toxic metals can disrupt the normal process. Currently, there are several ongoing investigations in the laboratory examining protein-metal including those that play important roles in a number of important biological processes. In addition, we are examining the interaction of a number of toxic metals such as mercury and lead with cellular proteins and how these interactions are associated with the toxicity of these metal. The proposed combination of structural and functional studies will provide information that is essential for understanding the role of protein-metal interactions in metal toxicity, insulin regulation, methylmercury remediation, microRNA regulation, tumour suppression and anti-HIV therapy.