1V2H

Crystal structure of human PNP complexed with guanine

Summary for 1V2H

• Entry DOI: 10.2210/pdb1v2h/pdb
• Related: 1M73 1PF7
• Descriptor: Purine nucleoside phosphorylase, SULFATE ION, GUANINE, ... (4 entities in total)
• Functional Keywords: purine nucleoside phosphorylase, drug design, synchrotron, guanine, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton (By similarity): P00491
• Total number of polymer chains: 1
• Total formula weight: 32589.06

Authors

De Azevedo Jr., W.F.,Canduri, F.,Pereira, J.H.,Dos Santos, D.M.,Bertacine Dias, M.V.,Silva, R.G.,Palma, M.S.,Basso, L.A.,Santos, D.S. (deposition date: 2003-10-16, release date: 2004-01-13, Last modification date: 2023-10-25)

Primary citation

de Azevedo Jr., W.F.,Canduri, F.,dos Santos, D.M.,Pereira, J.H.,Bertacine Dias, M.V.,Silva, R.G.,Mendes, M.A.,Basso, L.A.,Palma, M.S.,Santos, D.S.
Crystal structure of human PNP complexed with guanine.
Biochem.Biophys.Res.Commun., 312:767-772, 2003

PubMed Abstract: Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. PNP is a target for inhibitor development aiming at T-cell immune response modulation and has been submitted to extensive structure-based drug design. More recently, the 3-D structure of human PNP has been refined to 2.3A resolution, which allowed a redefinition of the residues involved in the substrate-binding sites and provided a more reliable model for structure-based design of inhibitors. This work reports crystallographic study of the complex of Human PNP:guanine (HsPNP:Gua) solved at 2.7A resolution using synchrotron radiation. Analysis of the structural differences among the HsPNP:Gua complex, PNP apoenzyme, and HsPNP:immucillin-H provides explanation for inhibitor binding, refines the purine-binding site, and can be used for future inhibitor design.

PubMed: 14680831
DOI: 10.1016/j.bbrc.2003.10.190

Experimental method

X-RAY DIFFRACTION (2.7 Å)