5l8o
From Proteopedia
crystal structure of human FABP6 in complex with cholate
Structural highlights
FunctionFABP6_HUMAN Ileal protein which stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. Isoform 2 is essential for the survival of colon cancer cells to bile acid-induced apoptosis.[1] Publication Abstract from PubMedFatty 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. Identification and Investigation of Novel Binding Fragments in the Fatty Acid Binding Protein 6 (FABP6).,Hendrick AG, Muller I, Willems H, Leonard PM, Irving S, Davenport R, Ito T, Reeves J, Wright S, Allen V, Wilkinson S, Heffron H, Bazin R, Turney J, Mitchell PJ J Med Chem. 2016 Aug 18. PMID:27500412[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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