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.
The N-terminal domain of 2, 3-cyclic nucleotide 3-phosphodiesterase harbours a GTP/ATP binding site / STINGO S; MASULLO M; POLVERINI E.; LAEZZA C; RUGGIERO I; ARCONE R; RUOZI E; DAL PIAZ F; MALFITANO A.M; DURSI A.M; BIFULCO M. - In: CHEMICAL BIOLOGY & DRUG DESIGN. - ISSN 1747-0277. - 70(2007), pp. 502-510. [10.1111/j.1747-0285.2007.00592.x]
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