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lüll Dealing with iron: common structural principles in proteins that transport iron and heme Baker HM; Anderson BF; Baker ENProc Natl Acad Sci U S A 2003[Apr]; 100 (7): 3579-83Iron is essential to life, but poses severe problems because of its toxicity and the insolubility of hydrated ferric ions at neutral pH. In animals, a family of proteins called transferrins are responsible for the sequestration, transport, and distribution of free iron. Comparison of the structure and function of transferrins with a completely unrelated protein hemopexin, which carries out the same function for heme, identifies molecular features that contribute to a successful protein system for iron acquisition, transport, and release. These include a two-domain protein structure with flexible hinges that allow these domains to enclose the bound ligand and provide suitable chemistry for stable binding and an appropriate trigger for release.|Binding Sites[MESH]|Carrier Proteins/*chemistry/metabolism[MESH]|Heme/*metabolism[MESH]|Hemopexin/chemistry/metabolism[MESH]|Iron/*metabolism[MESH]|Models, Molecular[MESH]|Protein Folding[MESH]|Protein Structure, Secondary[MESH]|Transferrin/metabolism[MESH] |