1rct Citations

Structures of human purine nucleoside phosphorylase complexed with inosine and ddI.

Biochem Biophys Res Commun 313 907-14 (2004)
Related entries: 1ula, 1ulb, 1v3q

Cited: 23 times
EuropePMC logo PMID: 14706628

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.

Reviews - 1rct mentioned but not cited (1)

  1. Augmentation Therapies as Treatments for Coexisting Somatic Problems in Schizophrenia-A Systematic Review. Dróżdż W, Wiciński M, Szota AM, Szambelan M, Radajewska I, Popławski I, Wojciechowski P. J Clin Med 12 4012 (2023)

Articles - 1rct mentioned but not cited (4)

  1. Four generations of transition-state analogues for human purine nucleoside phosphorylase. Ho MC, Shi W, Rinaldo-Matthis A, Tyler PC, Evans GB, Clinch K, Almo SC, Schramm VL. Proc Natl Acad Sci U S A 107 4805-4812 (2010)
  2. Design and directed evolution of a dideoxy purine nucleoside phosphorylase. Nannemann DP, Kaufmann KW, Meiler J, Bachmann BO. Protein Eng Des Sel 23 607-616 (2010)
  3. Functional and Structural Characterization of Purine Nucleoside Phosphorylase from Kluyveromyces lactis and Its Potential Applications in Reducing Purine Content in Food. Mahor D, Priyanka A, Prasad GS, Thakur KG. PLoS One 11 e0164279 (2016)
  4. Survey of ribose ring pucker of signaling nucleosides and nucleotides. Salmaso V, Jacobson KA. Nucleosides Nucleotides Nucleic Acids 39 322-341 (2020)


Reviews citing this publication (2)

Articles citing this publication (16)

  1. Nucleotide degradation and ribose salvage in yeast. Xu YF, Létisse F, Absalan F, Lu W, Kuznetsova E, Brown G, Caudy AA, Yakunin AF, Broach JR, Rabinowitz JD. Mol Syst Biol 9 665 (2013)
  2. Neighboring group participation in the transition state of human purine nucleoside phosphorylase. Murkin AS, Birck MR, Rinaldo-Matthis A, Shi W, Taylor EA, Almo SC, Schramm VL. Biochemistry 46 5038-5049 (2007)
  3. New catalytic mechanism for human purine nucleoside phosphorylase. Canduri F, Fadel V, Basso LA, Palma MS, Santos DS, de Azevedo WF. Biochem Biophys Res Commun 327 646-649 (2005)
  4. Kinetics and crystal structure of human purine nucleoside phosphorylase in complex with 7-methyl-6-thio-guanosine. Silva RG, Pereira JH, Canduri F, de Azevedo WF, Basso LA, Santos DS. Arch Biochem Biophys 442 49-58 (2005)
  5. Molecular modeling and dynamics simulations of PNP from Streptococcus agalactiae. Caceres RA, Saraiva Timmers LF, Dias R, Basso LA, Santos DS, de Azevedo WF. Bioorg Med Chem 16 4984-4993 (2008)
  6. Structural studies of human purine nucleoside phosphorylase: towards a new specific empirical scoring function. Timmers LF, Caceres RA, Vivan AL, Gava LM, Dias R, Ducati RG, Basso LA, Santos DS, de Azevedo WF. Arch Biochem Biophys 479 28-38 (2008)
  7. Crystal structure of human PNP complexed with hypoxanthine and sulfate ion. Canduri F, Fadel V, Dias MV, Basso LA, Palma MS, Santos DS, de Azevedo WF. Biochem Biophys Res Commun 326 335-338 (2005)
  8. Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin. Modrak-Wójcik A, Kirilenko A, Shugar D, Kierdaszuk B. Eur Biophys J 37 153-164 (2008)
  9. Association between arsenic metabolism gene polymorphisms and arsenic-induced skin lesions in individuals exposed to high-dose inorganic arsenic in northwest China. Luo L, Li Y, Gao Y, Zhao L, Feng H, Wei W, Qiu C, He Q, Zhang Y, Fu S, Sun D. Sci Rep 8 413 (2018)
  10. Dynamic changes in the proteome of human peripheral blood mononuclear cells with low dose ionizing radiation. Nishad S, Ghosh A. Mutat Res Genet Toxicol Environ Mutagen 797 9-20 (2016)
  11. Structural bioinformatics study of PNP from Schistosoma mansoni. da Silveira NJ, Uchôa HB, Canduri F, Pereira JH, Camera JC, Basso LA, Palma MS, Santos DS, de Azevedo WF. Biochem Biophys Res Commun 322 100-104 (2004)
  12. Constrained bonding environment in the Michaelis complex of Trypanosoma cruzi uridine phosphorylase. Silva RG, Kipp DR, Schramm VL. Biochemistry 51 6715-6717 (2012)
  13. Crystal structure of Escherichia coli purine nucleoside phosphorylase in complex with 7-deazahypoxanthine. Timofeev VI, Zhukhlistova NE, Abramchik YA, Fateev II, Kostromina MA, Muravieva TI, Esipov RS, Kuranova IP. Acta Crystallogr F Struct Biol Commun 74 355-362 (2018)
  14. Molecular modeling, dynamics and docking studies of purine nucleoside phosphorylase from Streptococcus pyogenes. Timmers LF, Caceres RA, Dias R, Basso LA, Santos DS, de Azevedo WF. Biophys Chem 142 7-16 (2009)
  15. Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir. Timofeev VI, Zhukhlistova NE, Abramchik YA, Muravieva TI, Esipov RS, Kuranova IP. Acta Crystallogr F Struct Biol Commun 74 402-409 (2018)
  16. Design and Synthesis of New Modified Flexible Purine Bases as Potential Inhibitors of Human PNP. Khandazhinskaya A, Fateev I, Eletskaya B, Maslova A, Konstantinova I, Seley-Radtke K, Kochetkov S, Matyugina E. Molecules 28 928 (2023)


Related citations provided by authors (1)

  1. Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors.. Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA Proc Natl Acad Sci U S A 88 11540-4 (1991)