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Backbone assignment of the apo-form of the human C-terminal domain of UDP-glucuronosyltransferase 1A (UGT1A).

Osborne MJ, Coutinho de Oliveira L, Volpon L, Borden KLB

Department of Pathology and Cell Biology, Institute of Research in Immunology and Cancer (IRIC), Université de Montréal, Pavilion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada.

A major component of phase II drug metabolism is the covalent addition of glucuronic acid to metabolites and xenobiotics. This activity is carried out by UDP-glucuronosyltransferases (UGT) which bind the UDP-glucuronic acid donor and catalyze the covalent addition of glucuronic acid sugar moieties onto a wide variety of substrates. UGTs play important roles in drug detoxification and were recently shown to act in an inducible form of multi-drug resistance in cancer patients. Despite their biological importance, structural understanding of these enzymes is limited. The C-terminal domain is identical for all UGT1A family members and required for binding to UDP-glucuronic acid as well as involved in contacts with substrates. Here, we report the backbone assignments for the C-terminal domain of UGT1A. These assignments are a critical tool for the development of a deeper biochemical understanding of substrate specificity and enzymatic activity.

Biomol NMR Assign 2018;12(2):315-318.

Pubmed ID: 29934866

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