3D1V

Crystal structure of human PNP complexed with 2-mercapto(3H) quinazolinone

3D1V の概要

• エントリーDOI: 10.2210/pdb3d1v/pdb
• 関連するPDBエントリー: 1m73 1pf7
• 分子名称: Purine nucleoside phosphorylase, SULFATE ION, 2-mercapto(3H)quinazolinone, ... (4 entities in total)
• 機能のキーワード: purine nucleoside phosphorylase, drug design, synchrotron, empirical scoring function, 2-mercapto-4(3h) quinazolinone, acetylation, disease mutation, glycosyltransferase, polymorphism, 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: 32651.28

構造登録者

De Azevedo Jr., W.F.,Basso, L.A.,Santos, D.S. (登録日: 2008-05-06, 公開日: 2009-07-14, 最終更新日: 2023-08-30)

主引用文献

Timmers, L.F.,Caceres, R.A.,Vivan, A.L.,Gava, L.M.,Dias, R.,Ducati, R.G.,Basso, L.A.,Santos, D.S.,de Azevedo, W.F.
Structural studies of human purine nucleoside phosphorylase: towards a new specific empirical scoring function
Arch.Biochem.Biophys., 479:28-38, 2008

PubMed Abstract: Human purine nucleoside phosphorylase (HsPNP) is a target for inhibitor development aiming at T-cell immune response modulation. In this work, we report the development of a new set of empirical scoring functions and its application to evaluate binding affinities and docking results. To test these new functions, we solved the structure of HsPNP and 2-mercapto-4(3H)-quinazolinone (HsPNP:MQU) binary complex at 2.7A resolution using synchrotron radiation, and used these functions to predict ligand position obtained in docking simulations. We also employed molecular dynamics simulations to analyze HsPNP in two conditions, as apoenzyme and in the binary complex form, in order to assess the structural features responsible for stability. Analysis of the structural differences between systems provides explanation for inhibitor binding. The use of these scoring functions to evaluate binding affinities and molecular docking results may be used to guide future efforts on virtual screening focused on HsPNP.

PubMed: 18790691
DOI: 10.1016/j.abb.2008.08.015

実験手法

X-RAY DIFFRACTION (2.7 Å)