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Crystal structure of human PNP complexed with guanine
- Source :
-
Biochemical & Biophysical Research Communications . Dec2003, Vol. 312 Issue 3, p767. 6p. - Publication Year :
- 2003
-
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 2.3 A˚ 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 2.7 A˚ 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. [Copyright &y& Elsevier]
- Subjects :
- *T cells
*IMMUNE response
*NUCLEOSIDES
*CRYSTALLOGRAPHY
Subjects
Details
- Language :
- English
- ISSN :
- 0006291X
- Volume :
- 312
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Biochemical & Biophysical Research Communications
- Publication Type :
- Academic Journal
- Accession number :
- 11469305
- Full Text :
- https://doi.org/10.1016/j.bbrc.2003.10.190