4KXN
Crystal structure of DNPH1 (RCL) with kinetine riboside monophosphate
Summary for 4KXN
| Entry DOI | 10.2210/pdb4kxn/pdb |
| Related | 4FYI 4KXL 4KXM |
| Descriptor | 2'-deoxynucleoside 5'-phosphate N-hydrolase 1, N-(furan-2-ylmethyl)adenosine 5'-(dihydrogen phosphate) (3 entities in total) |
| Functional Keywords | deoxyribonucleoside 5'-monophosphate n-glycosidase, hydrolase |
| Biological source | Rattus norvegicus (brown rat,rat,rats) |
| Cellular location | Cytoplasm (By similarity): O35820 |
| Total number of polymer chains | 4 |
| Total formula weight | 70402.56 |
| Authors | Padilla, A.,Labesse, G.,Kaminski, P.A. (deposition date: 2013-05-27, release date: 2014-02-05, Last modification date: 2023-09-20) |
| Primary citation | Amiable, C.,Pochet, S.,Padilla, A.,Labesse, G.,Kaminski, P.A. N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase DNPH1. Plos One, 8:e80755-e80755, 2013 Cited by PubMed Abstract: The gene dnph1 (or rcl) encodes a hydrolase that cleaves the 2'-deoxyribonucleoside 5'-monophosphate (dNMP) N-glycosidic bond to yield a free nucleobase and 2-deoxyribose 5-phosphate. Recently, the crystal structure of rat DNPH1, a potential target for anti-cancer therapies, suggested that various analogs of AMP may inhibit this enzyme. From this result, we asked whether N (6)-substituted AMPs, and among them, cytotoxic cytokinin riboside 5'-monophosphates, may inhibit DNPH1. Here, we characterized the structural and thermodynamic aspects of the interactions of these various analogs with DNPH1. Our results indicate that DNPH1 is inhibited by cytotoxic cytokinins at concentrations that inhibit cell growth. PubMed: 24260472DOI: 10.1371/journal.pone.0080755 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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