Related Experiment Video
Updated: Jun 24, 2025

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1
Published on: April 16, 2021
The N-terminal SAM domain of the dNTPase SAMHD1 is not required for inhibition by small molecule TH6342
Christopher Dirks1, Henri Colyn Bwanika1, Ann-Sofie Jemth1
1SciLifeLab, Department of Oncology-Pathology, Karolinska Institutet, Stockholm, Sweden.
Abstract:
Sterile alpha motif and histidine-aspartic acid domain containing protein-1 (SAMHD1) is a deoxynucleoside triphosphate (dNTP) hydrolase that controls dNTP pools and detoxifies cancer cells of chemotherapy metabolites. TH6342 is a recently reported small molecule inhibitor of SAMHD1 that interacts with the protein in vitro and non-competitively prevents dimerisation, a prerequisite for catalysis. The binding site of TH6342 on SAMHD1 is currently unknown. In the present study we demonstrate that the N-terminal SAM domain of SAMHD1 is not required for inhibition by TH6342.
Related Concept Videos
Restarting Stalled Replication Forks
siRNA - Small Interfering RNAs
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the...

