| Autor: |
Dirks, Christopher, Bwanika, Henri Colyn, Jemth, Ann-Sofie, Zhang, Si Min, Rudd, Sean G. |
| Předmět: |
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| Zdroj: |
Nucleosides, Nucleotides & Nucleic Acids; 2024, Vol. 43 Issue 8, p831-836, 6p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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