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1V3Q

Structure of human PNP complexed with DDI

Summary for 1V3Q
Entry DOI10.2210/pdb1v3q/pdb
Related1M73 1PF7 1RCT 1V41 1V45
DescriptorPurine nucleoside phosphorylase, SULFATE ION, 9-[(2R,5R)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-2-YL]-1,9-DIHYDRO-6H-PURIN-6-ONE, ... (4 entities in total)
Functional Keywordspurine nucleoside phosphorylase, drug design, synchrotorn, ddi, transferase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, cytoskeleton (By similarity): P00491
Total number of polymer chains1
Total formula weight32578.10
Authors
Canduri, F.,Pereira, J.H.,dos Santos, D.M.,Silva, R.G.,Palma, M.S.,Basso, L.A.,de Azevedo Jr., W.F.,Santos, D.S. (deposition date: 2003-11-04, release date: 2004-01-20, Last modification date: 2023-10-25)
Primary citationCanduri, F.,dos Santos, D.M.,Silva, R.G.,Mendes, M.A.,Basso, L.A.,Palma, M.S.,de Azevedo Jr., W.F.,Santos, D.S.
Structures of human purine nucleoside phosphorylase complexed with inosine and ddI
Biochem.Biophys.Res.Commun., 313:907-914, 2004
Cited by
PubMed Abstract: Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effect on B-cell function. PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides. The catalytic efficiency for inosine is 350,000-fold greater than for adenosine. Adenine nucleosides and nucleotides are deaminated by adenosine deaminase and AMP deaminase to their corresponding inosine derivatives which, in turn, may be further degraded. Here we report the crystal structures of human PNP in complex with inosine and 2('),3(')-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor design.
PubMed: 14706628
DOI: 10.1016/j.bbrc.2003.11.179
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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