Download MendeleyCrystal structure of human PNP complexed with guanine.
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.(2003) Biochem Biophys Res Commun 312: 767-772
- PubMed: 14680831
- DOI: https://doi.org/10.1016/j.bbrc.2003.10.190
- Primary Citation of Related Structures:
1V2H - 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.
Organizational Affiliation:
Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil. [email protected]
