4kxm

Crystal structure of DNPH1 (RCL) WITH N6-ISOPENTENYL-AMP

spinqualitylabelsall models 4kxm, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kxm is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.24Å Ligands: 6IA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNPH1_RAT Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases. Publication Abstract from PubMed 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. N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase DNPH1.,Amiable C, Pochet S, Padilla A, Labesse G, Kaminski PA PLoS One. 2013 Nov 19;8(11):e80755. doi: 10.1371/journal.pone.0080755., eCollection 2013. PMID:24260472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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