2KLH
NMR Structure of RCL in complex with GMP
Summary for 2KLH
| Entry DOI | 10.2210/pdb2klh/pdb |
| Descriptor | c-Myc-responsive protein Rcl, GUANOSINE-5'-MONOPHOSPHATE (2 entities in total) |
| Functional Keywords | protein, gmp, n-glycosidase, nucleus, phosphoprotein, hydrolase |
| Biological source | Rattus norvegicus (rat) |
| Cellular location | Cytoplasm (By similarity): O35820 |
| Total number of polymer chains | 2 |
| Total formula weight | 34987.06 |
| Authors | Padilla, A.,Yang, Y.,Labesse, G.,Zhang, C.,Kaminski, P.A. (deposition date: 2009-07-02, release date: 2009-10-20, Last modification date: 2024-05-29) |
| Primary citation | Yang, Y.,Padilla, A.,Zhang, C.,Labesse, G.,Kaminski, P.A. Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors J.Mol.Biol., 394:435-447, 2009 Cited by PubMed Abstract: The gene Rcl encodes a deoxynucleoside 5'-monophosphate N-glycosidase that catalyzes the hydrolysis of the N-glycosidic bond of the nucleotide to give deoxyribose 5-phosphate and a nucleobase, preferentially a purine. This enzyme is over-expressed in several cancers, and its rate of expression is correlated to the degree of aggressiveness of tumors, which makes it a new and attractive therapeutic target. We describe here its structural characterization in the presence of two inhibitory substrate mimics. One of these ligands corresponds to the monophosphorylated form of acyclovir, which is used in the clinic. This study reveals an important ligand-induced stabilization of the dimer structure of the enzyme. The original structural features of Rcl will be helpful for designing new inhibitors. PubMed: 19822152DOI: 10.1016/j.jmb.2009.10.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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