کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1953440 | 1057274 | 2006 | 8 صفحه PDF | دانلود رایگان |
Documenting the modes of interaction of uranyl (UO22+) 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.
Journal: Biochimie - Volume 88, Issue 11, November 2006, Pages 1631–1638