1V3Q

Structure of human PNP complexed with DDI

1V3Q の概要

• エントリーDOI: 10.2210/pdb1v3q/pdb
• 関連するPDBエントリー: 1M73 1PF7 1RCT 1V41 1V45
• 分子名称: Purine nucleoside phosphorylase, SULFATE ION, 9-[(2R,5R)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-2-YL]-1,9-DIHYDRO-6H-PURIN-6-ONE, ... (4 entities in total)
• 機能のキーワード: purine nucleoside phosphorylase, drug design, synchrotorn, ddi, 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: 32578.10

構造登録者

Canduri, F.,Pereira, J.H.,dos Santos, D.M.,Silva, R.G.,Palma, M.S.,Basso, L.A.,de Azevedo Jr., W.F.,Santos, D.S. (登録日: 2003-11-04, 公開日: 2004-01-20, 最終更新日: 2023-10-25)

主引用文献

Canduri, F.,dos Santos, D.M.,Silva, R.G.,Mendes, M.A.,Basso, L.A.,Palma, M.S.,de Azevedo Jr., W.F.,Santos, D.S.
Structures of human purine nucleoside phosphorylase complexed with inosine and ddI
Biochem.Biophys.Res.Commun., 313:907-914, 2004

PubMed Abstract: Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effect on B-cell function. PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides. The catalytic efficiency for inosine is 350,000-fold greater than for adenosine. Adenine nucleosides and nucleotides are deaminated by adenosine deaminase and AMP deaminase to their corresponding inosine derivatives which, in turn, may be further degraded. Here we report the crystal structures of human PNP in complex with inosine and 2('),3(')-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor design.

PubMed: 14706628
DOI: 10.1016/j.bbrc.2003.11.179

実験手法

X-RAY DIFFRACTION (2.8 Å)