1. Binding of transition metals to S100 proteins
- Author
-
Benjamin A. Gilston, Walter J. Chazin, and Eric P. Skaar
- Subjects
Models, Molecular ,inorganic chemicals ,0301 basic medicine ,Protein domain ,Plasma protein binding ,Biology ,Bioinformatics ,S100 protein ,DNA-binding protein ,Article ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,Protein Domains ,Environmental Science(all) ,Transition Elements ,Animals ,Humans ,Amino Acid Sequence ,General Environmental Science ,Manganese ,Agricultural and Biological Sciences(all) ,Sequence Homology, Amino Acid ,Biochemistry, Genetics and Molecular Biology(all) ,Binding protein ,S100 Proteins ,Cooperative binding ,S100 protein binding ,3. Good health ,Zinc ,030104 developmental biology ,Biophysics ,General Agricultural and Biological Sciences ,Copper ,Protein Binding ,Binding domain - Abstract
The S100 proteins are a unique class of EF-hand Ca(2+) binding proteins distributed in a cell-specific, tissue-specific, and cell cycle-specific manner in humans and other vertebrates. These proteins are distinguished by their distinctive homodimeric structure, both intracellular and extracellular functions, and the ability to bind transition metals at the dimer interface. Here we summarize current knowledge of S100 protein binding of Zn(2+), Cu(2+) and Mn(2+) ions, focusing on binding affinities, conformational changes that arise from metal binding, and the roles of transition metal binding in S100 protein function.
- Published
- 2016