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Article

Crystal structures of NUDT15 variants enabled by a potent inhibitor reveal the structural basis for thiopurine sensitivity.

The Journal of biological chemistry - 1 Jan 2000

Rehling Daniel, Zhang Si Min, Jemth Ann-Sofie, Koolmeister Tobias, Throup Adam, Wallner Olov, Scaletti Emma, Moriyama Takaya, Nishii Rina, Davies Jonathan, Desroses Matthieu, Rudd Sean G, Scobie Martin, Homan Evert, Berglund Ulrika Warpman, Yang Jun J, Helleday Thomas, Stenmark Pål

Abstract excerpt

The enzyme NUDT15 efficiently hydrolyzes the active metabolites of thiopurine drugs, which are routinely used for treating cancer and inflammatory diseases. Loss-of-function variants in NUDT15 are strongly associated with thiopurine intolerance, such as leukopenia, and preemptive NUDT15 genotyping has been clinically implemented to personalize thiopurine dosing. However, understanding the molecular consequences...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33753169
DOI: 10.1016/j.jbc.2021.100568
PMCID: PMC8079283

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