Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling
文献类型：期刊论文
| 作者 | Liu Yan3; Shi YanHong2 ; Liu XiaoXia3; Lin MingKun3; Lin DongHai2,3; Zhao YuFen1,3
|
| 刊名 | SCIENCE CHINA-CHEMISTRY
 |
| 出版日期 | 2010-09 |
| 卷号 | 53期号:9页码:1987-1993 |
| 关键词 | Ser-His cyclophilin A HSQC non-covalent interaction binding sites |
| ISSN号 | 1674-7291 |
| DOI | 10.1007/s11426-010-3192-z |
| 文献子类 | Article |
| 英文摘要 | Seryl-Histidine dipeptide (Ser-His) has been previously reported to be capable of cleaving DNAs and carboxyl esters, as well as proteins. The protein cleavage mechanism has not been addressed yet. As an initial step of protein cleavage activity, the non-covalent binding affinity of Ser-His for proteins is a crucial prerequisite. In this work, we took cyclophilin A (CyPA) as a substrate protein, and evaluated the non-covalent interaction between CyPA and Ser-His using a combination of NMR spectroscopy and molecular modeling approach. Two independent Ser-His binding sites on CyPA were detected using (15)N-(1)H heteronuclear single-quantum coherence (HSQC) spectra. Each binding site binds one Ser-His molecule. Dissociation constants, K (d1) and K (d2), were estimated to be 2.07 and 6.66 mmol/L, respectively, indicative of the weak non-covalent interaction between Ser-His and CyPA. Based on molecular modeling results, we suggest that both the alpha-amino and the side chain hydroxyl group of Ser-His are crucial for the non-covalent interaction between Ser-His and CyPA. This work sheds light on the molecular mechanism of Ser-His and its analogues cleaving proteins. |
| WOS关键词 | CIRCULAR-DICHROISM ; BINDING-PROTEIN ; TRIAD FORMS ; CLEAVAGE ; LIPASE ; SITE ; DNA ; ACETYLCHOLINESTERASE ; SUBSTRATE ; SUGGESTS |
| 资助项目 | National Natural Science Foundation of China[20732004] ; National Natural Science Foundation of China[30730026] ; National Natural Science Foundation of China[20805037] ; Ministry of Science and Technology of China[2007CB914304] |
| WOS研究方向 | Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:000282171900023 |
| 出版者 | SCIENCE PRESS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/278795]  |
| 专题 | 分析化学研究室 |
| 通讯作者 | Lin DongHai |
| 作者单位 | 1.Tsinghua Univ, Sch Life Sci & Engn, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Minist Educ,Dept Chem, Beijing 100084, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China; 3.Xiamen Univ, Coll Chem & Chem Engn, Key Lab Chem Biol Fujian Prov, Dept Chem Biol,Dept Chem, Xiamen 361005, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Liu Yan,Shi YanHong,Liu XiaoXia,et al. Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling[J]. SCIENCE CHINA-CHEMISTRY,2010,53(9):1987-1993. |
| APA | Liu Yan,Shi YanHong,Liu XiaoXia,Lin MingKun,Lin DongHai,&Zhao YuFen.(2010).Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling.SCIENCE CHINA-CHEMISTRY,53(9),1987-1993. |
| MLA | Liu Yan,et al."Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling".SCIENCE CHINA-CHEMISTRY 53.9(2010):1987-1993. |
入库方式： OAI收割
来源：上海药物研究所
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