1M73: Crystal Structure Of Human Pnp At 2.3a Resolution

Citation:
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.
PDB ID: 1M73Download
MMDB ID: 24605
PDB Deposition Date: 2002/7/18
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1M73: trimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1M73
Label Count Molecule
Proteins (3 molecules)
3
Purine Nucleoside Phosphorylase(Gene symbol: PNP)
Molecule annotation
Chemicals (9 molecules)
1
9
* Click molecule labels to explore molecular sequence information.

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