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- Title
The N-Terminal Domain of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase Harbors a GTP/ATP Binding Site.
- Authors
Stingo, Stefania; Masullo, Mariorosario; Polverini, Eugenia; Laezza, Chiara; Ruggiero, Immacolata; Arcone, Rosaria; Ruozi, Enrica; Piaz, Fabrizio Dal; Malfitano, Anna Maria; D'Ursi, Anna Maria; Bifulco, Maurizio
- Abstract
The interaction between 2′,3′-cyclic nucleotide 3′-phosphodiesterase and guanine/adenine nucleotides was investigated. The binding of purine nucleotides to 2′,3′-cyclic nucleotide 3′-phosphodiesterase was revealed by both direct and indirect methods. In fact, surface plasmon resonance experiments, triphosphatase activity measurements, and fluorescence experiments revealed that 2′,3′-cyclic nucleotide 3′-phosphodiesterase binds purine nucleotide triphosphates with an affinity higher than that displayed for diphosphates; on the contrary, the affinity for both purine monophosphates and pyrimidine nucleotides was negligible. An interpretation of biological experimental data was achieved by a building of 2′,3′-cyclic nucleotide 3′-phosphodiesterase N-terminal molecular model. The structural elements responsible for nucleotide binding were identified and potential complexes between the N-terminal domain of CNP-ase and nucleotide were analyzed by docking simulations. Therefore, our findings suggest new functional and structural property of the N-terminal domain of CNPase.
- Subjects
CYCLIC nucleotide phosphodiesterases; GUANOSINE triphosphate; ADENOSINE triphosphate; LIGAND binding (Biochemistry); PURINE nucleotides; SURFACE plasmon resonance; MOLECULAR models
- Publication
Chemical Biology & Drug Design, 2007, Vol 70, Issue 6, p502
- ISSN
1747-0277
- Publication type
Article
- DOI
10.1111/j.1747-0285.2007.00592.x