Eg5, a mitotic kinesin exclusively involved inthe formation and function of the mitotic spindle has attracted interest as ananticancer drug target. Eg5 is co-crystallized with several inhibitors bound toits allosteric binding pocket. Each of these occupies a pocket formed byloop5/helix a2.Recently designed inhibitors additionally occupy a hydrophobic pocket of thissite. The goal of the present study was to identify new fragments which fillthis hydrophobic pocket and might be interesting chemical moieties to designnew inhibitors.

Mitotic kinesin Eg5 inhibitors generation by computational MED-portion based drug design at PDB scale

239th National Meeting (2010)

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