Hendrick, Alan G. Müller, Ilka Willems, Henriëtte Leonard, Philip M. Irving, Steve Davenport, Richard Ito, Takashi Reeves, Jenny Wright, Susanne Allen, Vivienne Wilkinson, Stephen Heffron, Helen Bazin, Richard Turney, Jennifer Mitchell, Philip J. Identification and Investigation of Novel Binding Fragments in the Fatty Acid Binding Protein 6 (FABP6) Fatty acid binding protein 6 (FABP6) is a potential drug discovery target, which, if inhibited, may have a therapeutic benefit for the treatment of diabetes. Currently, there are no published inhibitors of FABP6, and with the target believed to be amenable to fragment-based drug discovery, a structurally enabled program was initiated. This program successfully identified fragment hits using the surface plasmon resonance (SPR) platform. Several hits were validated with SAR and were found to be displaced by the natural ligand taurocholate. We report the first crystal structure of human FABP6 in the unbound form, in complex with cholate, and with one of the key fragments. surface plasmon resonance;crystal structure;Fatty;SPR;program;SAR;Binding Protein 6;fragment hits;Novel Binding Fragments;ligand taurocholate;fragment-based drug discovery;FABP 6;drug discovery target;Several hits 2016-08-08
    https://acs.figshare.com/articles/dataset/Identification_and_Investigation_of_Novel_Binding_Fragments_in_the_Fatty_Acid_Binding_Protein_6_FABP6_/3644595
10.1021/acs.jmedchem.6b00869.s002