BIOL 232 |
| Many methods for the prediction of interaction sites in protein 3D structures are not very selective and have low precision. This problem is addressed using THEMATICS, a simple computational method for identification of active sites in protein structures. Using a test set of 169 enzymes from the Catalytic Site Atlas, it is shown that THEMATICS can deliver precise, localized site predictions. Adjustment of the cut-off criteria can improve recall rates for catalytic residues with only a small sacrifice in precision. With a preferred cut-off value of 0.99, THEMATICS achieves a high success rate of 93% for interaction site prediction. Recall rates for catalytic residue prediction are similar to those of other structure-based methods, but with two- to five- fold better precision and a low false positive rate of only 3%. This good performance is observed across the six E.C. classes and for unbound as well as bound structures. |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |