title: Structural insights into protein-uranyl interaction: towards an in silico detection method.
abstract: Documenting the modes of interaction of uranyl (UO(2)2+) with large biomolecules, and particularly with proteins, is instrumental for the interpretation of its behavior in vitro and in vivo. The gathering of three-dimensional information concerning uranyl-first shell atoms from two structural databases, the Cambridge Structural Databank and the Protein Data Bank (PDB) allowed a screening of corresponding topologies in proteins of known structure. In the computer-aided procedure, all potentially bound residues from the template structure were granted full flexibility using a rotamer library. The Amber force-field was used to loosen constraints and score each predicted site. Our algorithm was validated as a first stage through the recognition of existing experimental data in the PDB. The coherent localization of missing atoms in the density map of an ambiguous uranium/uranyl-protein complex exemplified the efficiency of our approach, which is currently suggesting the experimental investigation of uranyl-protein binding site.
authors.affiliation: CEA VALRHO, DSV-DIEP-SBTN, Service de Biochimie postgénomique et Toxicologie Nucléaire, 30207 Bagnols-sur-Cèze, France. olivier.pible@cea.fr
authors.forename: O
authors.initials: O
authors.lastname: Pible
authors.forename: P
authors.initials: P
authors.lastname: Guilbaud
authors.forename: J-L
authors.initials: JL
authors.lastname: Pellequer
authors.forename: C
authors.initials: C
authors.lastname: Vidaud
authors.forename: E
authors.initials: E
authors.lastname: Quéméneur
mesh_terms: D003201:Computers; D007700:Kinetics; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D012984:Software; D014501:Uranium / Q000737:chemistry*
chemical_list: D011506:Proteins; D014501:Uranium