10.1021/acs.jmedchem.6b00869.s002
Alan G. Hendrick
Alan G.
Hendrick
Ilka Müller
Ilka
Müller
Henriëtte Willems
Henriëtte
Willems
Philip
M. Leonard
Philip
M.
Leonard
Steve Irving
Steve
Irving
Richard Davenport
Richard
Davenport
Takashi Ito
Takashi
Ito
Jenny Reeves
Jenny
Reeves
Susanne Wright
Susanne
Wright
Vivienne Allen
Vivienne
Allen
Stephen Wilkinson
Stephen
Wilkinson
Helen Heffron
Helen
Heffron
Richard Bazin
Richard
Bazin
Jennifer Turney
Jennifer
Turney
Philip
J. Mitchell
Philip
J.
Mitchell
Identification
and Investigation of Novel Binding
Fragments in the Fatty Acid Binding Protein 6 (FABP6)
American Chemical Society
2016
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 00:00:00
Dataset
https://acs.figshare.com/articles/dataset/Identification_and_Investigation_of_Novel_Binding_Fragments_in_the_Fatty_Acid_Binding_Protein_6_FABP6_/3644595
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.