Advances in Metal Binding Proteins

Dear Colleagues,

Everyone knows that the functioning of any biological system is impossible without metal ions. The ‘metals of life’ include sodium, potassium, magnesium, calcium, manganese, iron, cobalt, zinc, nickel, vanadium, molybdenum, and tungsten. Any biological system contains special proteins specifically interacting with metal ions. Metal ions play several major roles in proteins: structural, regulatory, and enzymatic. Strong binding of some metal ions increases the stability of proteins or protein domains. Some metal ions can regulate various cell processes being first, second, or third messengers. Calcium is the most universal carrier of signals to cells. It regulates all important aspects of cell activity, beginning with fertilization and ending with apoptotic suicide at the end of the life cycle. Metal ions are an essential part of many enzymes and are indispensable in many catalytic reactions.

Despite the apparent good knowledge of the structure and properties of many metal-binding proteins, many aspects of their structure and, in particular, mechanisms of their functioning are still insufficiently studied. For example, although the three-dimensional structure of many calcium-binding sites in proteins is well known, a closer look at their environment reveals common structural features in these proteins that were not previously noticed. Studying the interactions of metal binding proteins with proteins of other classes allows us to reach a better understanding of their physiological functions. Modern methods of genetic engineering and knowledge of the three-dimensional structure of metal-binding proteins allow us to study their structure and functions at a new level. The obtained fundamental knowledge can already be used in applied science. Comprehensive reviews or original research articles are most welcome.

Dr. Eugene Permyakov
Collection Editor

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