Theoretical Design of Catalytic Domain of Abzyme Se-scFv2F3 by Introducing a Catalytic Triad

作     者：LUO Quan, ZHOU Yi-han, YAO Yuan and LI Ze-sheng State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130021, P. R. China 

作者机构：Institute of Theoretical ChemistryJilin University State Key Laboratory of Theoretical and Computational Chemistry Jilin Changchun 130021 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究(英文版))

年 卷 期：2010年第26卷第1期

页      面：118-121页

核心收录：

学科分类：081705[工学-工业催化] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学] 

基　　金：Supported by the National Natural Science Foundation of China(Nos.20333050,20673044) Program for Changjiang Scho-lars and Innovative Research Team in University of China(No.IRT0625) Key Subject of Science and Technology by Jilin Province,China 

主　　题：Abzyme scFv2F3 Homology modeling Molecular dynamics simulation 

摘      要：The single chain antibody scFv2F3 can be converted into selenium-containing Se-scFv2F3 by chemical mutation of the Ser residues. With antibody fragment 1NQB as a template, the catalytic domain of scFv2F3 was built by using homology modeling and molecular dynamics(MD) simulations. On the basis of the 3D model, we discussed the importance of Ser52 as the chemical modification site and redesigned the protein groups nearby Ser52 via introducing a catalytic triad. The following 10 ns MD results show that the designed Ser52-Trp29-Gln72 catalytic triad is stable enough and high close to the local structural features of native glutathione peroxidases(GPX). Our results may be useful for creating a new abzyme with higher catalytic efficiency and stability.