Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods
文献类型：期刊论文
| 作者 | Zhu, Kongkai2; Jiang, Cheng-Shi2; Hu, Junchi1,3; Liu, Xigong2; Yan, Xue2; Tao, Hongrui2; Luo, Cheng1 ; Zhang, Hua2
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| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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| 出版日期 | 2018 |
| 卷号 | 495期号:1页码:721-727 |
| 关键词 | PRMT5 SAM competitive inhibitor Molecular docking Molecular dynamics simulation Molecular mechanics/Poisson-Boltzmann surface area PRMT5:MEP50 interaction |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2017.11.089 |
| 文献子类 | Article |
| 英文摘要 | Protein arginine methyltransferase 5 (PRMT5) is the most promising anticancer target in PRMT family. In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods. Previously reported CMP5 was also thought of as a SAM competitive inhibitor of PRMT5, but the direct inhibition activity against PRMT5 at enzymatic level was not provided. Therefore, we tested the half-maximal inhibitory concentration (IC50) of CMP5 against PRMT5 at enzymatic level for the purpose of summarizing the interaction characteristics of SAM binding site inhibitors with PRMT5. Additionally, as the essential interacting partner of PRMT5, the binding attributes of the WD-repeat-containing protein MEP50 (methylosome protein 50) was investigated, and nine key residues that contribute most to PRMT5:MEP50 interaction were identified. These results could be helpful in discovering new potent and specific inhibitors of PRMT5, as well as in designing mutant residue assay to modulate the catalytic activity of PRMT5. (C) 2017 Elsevier Inc. All rights reserved. |
| WOS关键词 | MOLECULAR-DYNAMICS ; ACCURATE DOCKING ; PRMT5 ; METHYLATION ; OPTIMIZATION ; DISCOVERY ; TARGETS ; GLIDE |
| 资助项目 | Natural Science Foundation of Shandong Province[ZR2017BH038] ; Natural Science Foundation of Shandong Province[JQ201721] ; Young Taishan Scholars Program[tsqn20161037] ; Shandong Talents Team Cultivation Plan of University Preponderant Discipline[10027] ; Natural Science Foundation of China[21672082] ; Shandong Key Development Project[2016GSF201209] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000423897600110 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/272334]  |
| 专题 | 药物发现与设计中心 中科院受体结构与功能重点实验室 新药研究国家重点实验室 |
| 通讯作者 | Luo, Cheng; Zhang, Hua |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Drug Discovery & Design Ctr, Shanghai 201203, Peoples R China; 2.Univ Jinan, Sch Biol Sci & Technol, Jinan 250022, Shandong, Peoples R China; 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhu, Kongkai,Jiang, Cheng-Shi,Hu, Junchi,et al. Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2018,495(1):721-727. |
| APA | Zhu, Kongkai.,Jiang, Cheng-Shi.,Hu, Junchi.,Liu, Xigong.,Yan, Xue.,...&Zhang, Hua.(2018).Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,495(1),721-727. |
| MLA | Zhu, Kongkai,et al."Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 495.1(2018):721-727. |
入库方式： OAI收割
来源：上海药物研究所
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