Abstract
TGR5, the G protein coupled bile acid receptor, is involved in bile homeostasis, inflammatory responses and is linked to hepatobiliary diseases. Therefore targeted therapy involving inhibition of TGR5 is of immense interest. However, up to date no solved structure of TGR5 exists and oligomerization properties are largely unknown. Our aim is to determine TGR5 structural changes and oligomerization by three approaches including fluorophor coupled TGR5 plasmids, ACP tagged TGR5 and incorporation of unnatural amino acids for site specific labeling with a Forster Resonance energy transfer (FRET) dye.
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