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Comparison of Properties of Tumor Necrosis Factor-α Converting Enzyme (TACE) and Some Matrix Metalloproteases (MMPs) in Catalytic Domains
引用本文:赵云斌,冯文芳,杨渝珍,凌伦奖,陈润生.Comparison of Properties of Tumor Necrosis Factor-α Converting Enzyme (TACE) and Some Matrix Metalloproteases (MMPs) in Catalytic Domains[J].华中科技大学学报(医学英德文版),2006,26(6):637-639.
作者姓名:赵云斌  冯文芳  杨渝珍  凌伦奖  陈润生
作者单位:Department of Chemistry Huazhong University of Science and Technology,Department of Chemistry Huazhong University of Science and Technology,Department of Biochemistry and Molecular Biology Tongji Medical College Huazhong University of Science and Technology,Institute of Biophysics Academia Sinica,Institute of Biophysics Academia Sinica,Wuhan 430074 China,Wuhan 430074 China,Wuhan 430030 China,Beijing 100101 China,Beijing 100101 China
基金项目:This work was supported by a grant from the National Nature Science Foundation of China (Grants No.31371309).
摘    要:Tumor necrosis factor-α (TNF-α) is a critical cyto-kine in organism. It has been discovered that elevated TNF-α levels are implicated in a number of chronic dis-eases such as rheumatoid arthritis, multiple sclerosis, type II diabetes, inflammatory bowel disease, and other human ailments1]. The recent clinical successes of monoclonal TNF-α antibody Infliximab2] and the soluble TNF p75 receptor fusion protein Entanercept3] in RA patients suggest that anti-TNF-α is a valid target …

关 键 词:tumor  necrosis  factor-α  converting  enzyme  matrix  metalloprotease  catalytic  domain
收稿时间:2006-08-20
修稿时间:2006-08-20

Comparison of properties of tumor necrosis factor-α converting enzyme (TACE) and some matrix metalloproteases (MMPs) in catalytic domains
Yunbin Zhao,Wenfang Feng,Yuzhen Yang,Lunjiang Ling,Runsheng Chen.Comparison of properties of tumor necrosis factor-α converting enzyme (TACE) and some matrix metalloproteases (MMPs) in catalytic domains[J].Journal of Zuazhong University of Science and Technology: Medical Edition,2006,26(6):637-639.
Authors:Yunbin Zhao  Wenfang Feng  Yuzhen Yang  Lunjiang Ling  Runsheng Chen
Institution:(1) Department of Chemistry, Huazhong University of Science and Technology, Wuhan, 430074, China;(2) Department of Biochemistry and Molecular Biology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, China;(3) Institute of Biophysics Academia Sinica, Beijing, 100101, China
Abstract:Summary The crystal structural data of TACE, MMP-1, MMP-2, MMP-3 and MMP-9 were obtained from PDB database, and then their catalytic domains’ properties including conformation, molecular surface hydrophobicity and electrostatic potential were analyzed and compared by using Insight II molecular modeling software. It was found that the conformation and molecular surface hydrophobicity of catalytic domains of TACE and MMPs were not obviously different, but the molecular surface electrostatic potential of catalytic domain of TACE and MMPs had obvious differences. The findings are helpful in the Rational Drug Design of TACE selective inhibitor. This work was supported by a grant from the National Nature Science Foundation of China (Grants No.31371309).
Keywords:tumor necrosis factor-or converting enzyme  matrix metalloprotease  catalytic domain
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