title: Binding of transition metals to S100 proteins.
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.
authors.affiliation: Departments of Biochemistry and Chemistry, and Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232-9717, USA.
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Gilston
authors.affiliation: Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN, 37232-2561, USA.
authors.forename: Eric P
authors.initials: EP
authors.lastname: Skaar
authors.affiliation: Departments of Biochemistry and Chemistry, and Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232-9717, USA. walter.chazin@vanderbilt.edu.
authors.forename: Walter J
authors.initials: WJ
authors.lastname: Chazin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003300:Copper / Q000378:metabolism*; D006801:Humans; D008345:Manganese / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D000072417:Protein Domains; D009418:S100 Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D028561:Transition Elements / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
chemical_list: D009418:S100 Proteins; D028561:Transition Elements; D008345:Manganese; D003300:Copper; D015032:Zinc
keywords: Copper; Manganese; S100 Proteins; Zinc