1M73
CRYSTAL STRUCTURE OF HUMAN PNP AT 2.3A RESOLUTION
Summary for 1M73
| Entry DOI | 10.2210/pdb1m73/pdb |
| Related | 1ULA |
| Descriptor | PURINE NUCLEOSIDE PHOSPHORYLASE, SULFATE ION (3 entities in total) |
| Functional Keywords | purine nucleoside phosphorylase, drug design, synchrotron, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytoskeleton (By similarity): P00491 |
| Total number of polymer chains | 1 |
| Total formula weight | 32341.87 |
| Authors | De Azevedo Jr., W.F.,Marangoni Dos Santos, D.,Canduri, F.,Santos, G.C.,Olivieri, J.R.,Silva, R.G.,Basso, L.A.,Palma, M.S.,Santos, D.S. (deposition date: 2002-07-18, release date: 2003-09-16, Last modification date: 2023-10-25) |
| Primary citation | de Azevedo, W.F.,Canduri, F.,dos Santos, D.M.,Silva, R.G.,de Oliveira, J.S.,de Carvalho, L.P.,Basso, L.A.,Mendes, M.A.,Palma, M.S.,Santos, D.S. Crystal structure of human purine nucleoside phosphorylase at 2.3A resolution. Biochem.Biophys.Res.Commun., 308:545-552, 2003 Cited by PubMed Abstract: Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. In human, PNP is the only route for degradation of deoxyguanosine and genetic deficiency of this enzyme leads to profound T-cell mediated immunosuppression. PNP is therefore a target for inhibitor development aiming at T-cell immune response modulation and its low resolution structure has been used for drug design. Here we report the structure of human PNP solved to 2.3A resolution using synchrotron radiation and cryocrystallographic techniques. This structure allowed a more precise analysis of the active site, generating a more reliable model for substrate binding. The higher resolution data allowed the identification of water molecules in the active site, which suggests binding partners for potential ligands. Furthermore, the present structure may be used in the new structure-based design of PNP inhibitors. PubMed: 12914785DOI: 10.1016/S0006-291X(03)01431-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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