WP6 combines the cristallographic expertise of Dr. Alejandro Buschiazzo, head of the Protein Crystallography laboratory at the Pasteur Institute in Montevideo, Uruguay with the bio-informatic expertise of three principal investigators, Dr. Alia Benkhala (Institut Pasteur of Tunis, IPT), Dr. Cedric Notredame (Centre for Genomic Regulation (CRG) ,Barcelona), and Prof. Manuela Helmer-Citterich (University of Rome Tor Vergata, UR2). WP6 aims to provide accurate, high resolution, three-dimensional structures of those target proteins identified and validated by partners 1, 5, and 11 using X ray diffraction crystallography (partner 4). In silico approaches established by the consortium partners 3, 7 and 9 will be used to assess the druggability of novel targets and prioritize structural analysis, and to improve the characterization of the Leishmania kinome complement through comparative genomics [51-53], sequence comparison and phylogenetic  and structural analysis    . Recent genomic studies of three trypanosomes have shown the presence of a rich and complex kinome complement within these parasites . We intend to take this characterization further and use the resulting kinome classification to prioritize potential drug targets for in vitro and in vivo testing (partners 1, 6, and 10). We also intend to build on existing SAR (Structure/Activity Relationship) analysis  to provide the consortium with potential drug leads that could be tested in vitro (partner 1 and 10) and in vivo (partner 6). While the first step will be to insure an exhaustive identification of all Leishmania protein kinases and build upon potential novel, experimentally identified kinases (partners 1 and 5), later contributions will include bioinformatic support for structure-based drug design (partners 4 and 10). As soon as experimental structures of target kinases in complex with active ligands become available from partner 4, an iterative association will be established within WP6 to use this information in further in silico modeling of modified ligands attempting to catalyze the ‘active to lead’ stage.