title: Computational design of metalloproteins.
abstract: A number of design strategies exist for the development of novel metalloproteins. These strategies often exploit the inherent symmetry of metal coordination and local topology. Computational design of metal binding sites in flexible regions of proteins is challenging as the number of conformational degrees of freedom is significantly increased. Additionally, without pre-organization of the primary shell ligands by the protein fold, metal binding sites can rearrange according to the coordination constraints of the metal center. Examples of metal incorporation into existing folds, full fold design exploiting symmetry, and fold design in asymmetric scaffolds are presented.
authors.affiliation: Department of Biochemistry and Molecular Biology, Center for Advanced Biotechnology and Medicine, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, 679 Hoes Lane West, Piscataway, NJ, 08854, USA.
authors.forename: Avanish S
authors.initials: AS
authors.lastname: Parmar
authors.forename: Douglas
authors.initials: D
authors.lastname: Pike
authors.forename: Vikas
authors.initials: V
authors.lastname: Nanda
mesh_terms: D001665:Binding Sites; D019295:Computational Biology / Q000379:methods; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry
chemical_list: D008024:Ligands; D008667:Metalloproteins; D008670:Metals