1M73

CRYSTAL STRUCTURE OF HUMAN PNP AT 2.3A RESOLUTION

1M73 の概要

• エントリーDOI: 10.2210/pdb1m73/pdb
• 関連するPDBエントリー: 1ULA
• 分子名称: PURINE NUCLEOSIDE PHOSPHORYLASE, SULFATE ION (3 entities in total)
• 機能のキーワード: purine nucleoside phosphorylase, drug design, synchrotron, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): P00491
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32341.87

構造登録者

De Azevedo Jr., W.F.,Marangoni Dos Santos, D.,Canduri, F.,Santos, G.C.,Olivieri, J.R.,Silva, R.G.,Basso, L.A.,Palma, M.S.,Santos, D.S. (登録日: 2002-07-18, 公開日: 2003-09-16, 最終更新日: 2023-10-25)

主引用文献

de Azevedo, W.F.,Canduri, F.,dos Santos, D.M.,Silva, R.G.,de Oliveira, J.S.,de Carvalho, L.P.,Basso, L.A.,Mendes, M.A.,Palma, M.S.,Santos, D.S.
Crystal structure of human purine nucleoside phosphorylase at 2.3A resolution.
Biochem.Biophys.Res.Commun., 308:545-552, 2003

PubMed Abstract: Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. In human, PNP is the only route for degradation of deoxyguanosine and genetic deficiency of this enzyme leads to profound T-cell mediated immunosuppression. PNP is therefore a target for inhibitor development aiming at T-cell immune response modulation and its low resolution structure has been used for drug design. Here we report the structure of human PNP solved to 2.3A resolution using synchrotron radiation and cryocrystallographic techniques. This structure allowed a more precise analysis of the active site, generating a more reliable model for substrate binding. The higher resolution data allowed the identification of water molecules in the active site, which suggests binding partners for potential ligands. Furthermore, the present structure may be used in the new structure-based design of PNP inhibitors.

PubMed: 12914785
DOI: 10.1016/S0006-291X(03)01431-1

実験手法

X-RAY DIFFRACTION (2.3 Å)