6C01
Human ectonucleotide pyrophosphatase / phosphodiesterase 3 (ENPP3, NPP3, CD203c)
Summary for 6C01
| Entry DOI | 10.2210/pdb6c01/pdb |
| Descriptor | Ectonucleotide pyrophosphatase/phosphodiesterase family member 3, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
| Functional Keywords | phosphodiesterase, nucleotide, zinc, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 203612.14 |
| Authors | Gorelik, A.,Randriamihaja, A.,Illes, K.,Nagar, B. (deposition date: 2017-12-27, release date: 2018-05-02, Last modification date: 2024-10-23) |
| Primary citation | Gorelik, A.,Randriamihaja, A.,Illes, K.,Nagar, B. Structural basis for nucleotide recognition by the ectoenzyme CD203c. FEBS J., 285:2481-2494, 2018 Cited by PubMed Abstract: The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides. CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells. Multiple other roles and substrates have also been proposed for this protein. In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog. The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands. Dimerization of the protein does not affect its catalytic activity. These findings expand our understanding of substrate recognition within the NPP family. PubMed: 29717535DOI: 10.1111/febs.14489 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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