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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor.

Calf spleen purine nucleoside phosphorylase was purified to homogeneity and its amino acid sequence was determined. The complex of the enzyme with an N(7)-acycloguanosine inhibitor crystallized in the cubic space group P2(1)3, with unit cell dimension a = 94.02 A and one monomer in the asymmetric crystal unit. The biologically active trimer is formed by the crystallographic three-fold axis. The structure was solved by molecular replacement methods, using the model of the human erythrocyte enzyme, and refined at a resolution of 2.9 A to an R-factor of 0.21. The orientation of the inhibitor at the active site is examined in relation to the catalytic activity of the enzyme in the phosphorolysis of N(7)-beta-D-purine nucleosides.[1]

References

  1. Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor. Bzowska, A., Luić, M., Schröder, W., Shugar, D., Saenger, W., Koellner, G. FEBS Lett. (1995) [Pubmed]
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