1PF7

CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH IMMUCILLIN H

1PF7 の概要

• エントリーDOI: 10.2210/pdb1pf7/pdb
• 関連するPDBエントリー: 1M73
• 分子名称: PURINE NUCLEOSIDE PHOSPHORYLASE, SULFATE ION, 1,4-DIDEOXY-4-AZA-1-(S)-(9-DEAZAHYPOXANTHIN-9-YL)-D-RIBITOL, ... (4 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: 32739.32

構造登録者

De Azevedo Jr., W.F.,Canduri, F.,Dos Santos, D.M.,Pereira, J.H.,Dias, M.V.B.,Silva, R.G.,Mendes, M.A.,Palma, M.S.,Basso, L.A.,Santos, D.S. (登録日: 2003-05-24, 公開日: 2004-06-01, 最終更新日: 2023-09-20)

主引用文献

De Azevedo Jr., W.F.,Canduri, F.,Dos Santos, D.M.,Pereira, J.H.,Dias, M.V.B.,Silva, R.G.,Mendes, M.A.,Palma, M.S.,Basso, L.A.,Santos, D.S.
Structural basis for inhibition of human PNP by immucillin-H
Biochem.Biophys.Res.Commun., 309:917-922, 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. This work reports on the crystallographic study of the complex of human PNP-immucillin-H (HsPNP-ImmH) solved at 2.6A resolution using synchrotron radiation. Immucillin-H (ImmH) inhibits the growth of malignant T-cell lines in the presence of deoxyguanosine without affecting non-T-cell tumor lines. ImmH inhibits activated normal human T cells after antigenic stimulation in vitro. These biological effects of ImmH suggest that this agent may have utility in the treatment of certain human diseases characterized by abnormal T-cell growth or activation. This is the first structural report of human PNP complexed with immucillin-H. The comparison of the complex HsPNP-ImmH with recent crystallographic structures of human PNP explains the high specificity of immucillin-H for human PNP.

PubMed: 13679061
DOI: 10.1016/j.bbrc.2003.08.094

実験手法

X-RAY DIFFRACTION (2.6 Å)