Skip to Main content Skip to Navigation
New interface
Journal articles

Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors.

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.
Complete list of metadata

https://hal-pasteur.archives-ouvertes.fr/pasteur-03726707
Contributor : André PADILLA Connect in order to contact the contributor
Submitted on : Monday, July 18, 2022 - 5:59:55 PM
Last modification on : Friday, October 14, 2022 - 5:59:52 PM

Identifiers

Collections

Citation

Yinshan Yang, André Padilla, Chi Zhang, Gilles Labesse, Pierre-Alexandre Kaminski. Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors.. Journal of Molecular Biology, 2009, 394 (3), pp.435-47. ⟨10.1016/j.jmb.2009.10.004⟩. ⟨pasteur-03726707⟩

Share

Metrics

Record views

13