Crystal structures of sirt3 reveal that the alpha 2-alpha 3 loop and alpha 3-helix affect the interaction with long-chain acyl lysine
文献类型：期刊论文
| 作者 | Gai, Wei1,2; Li, He2,3; Jiang, Hualiang2,4; Long, Yaqiu2,3; Liu, Dongxiang1,2 |
| 刊名 | Febs letters
 |
| 出版日期 | 2016-09-01 |
| 卷号 | 590期号:17页码:3019-3028 |
| 关键词 | Allosteric site Deacylation Inhibitor Long-chain fatty acid Sirtuins |
| ISSN号 | 0014-5793 |
| DOI | 10.1002/1873-3468.12345 |
| 通讯作者 | Long, yaqiu(yqlong@mail.simm.ac.cn) ; Liu, dongxiang(dxl@mail.shcnc.ac.cn) |
| 英文摘要 | Sirt1-7 play important roles in many biological processes and age-related diseases. in addition to a nad(+)-dependent deacetylase activity, they can catalyze several other reactions, including the hydrolysis of long-chain fatty acyl lysine. to study the binding modes of sirtuins to long-chain acyl lysines, we solved the crystal structures of sirt3 bound to either a h3k9-myristoylated-or a h3k9-palmitoylated peptide. interaction of sirt3 with the palmitoyl group led to unfolding of the alpha 3-helix. the myristoyl and palmitoyl groups bind to the c-pocket and an allosteric site near the alpha 3-helix, respectively. we found that the residues preceding the alpha 3-helix determine the size of the c-pocket. the flexibility of the alpha 2-alpha 3 loop and the plasticity of the alpha 3-helix affect the interaction with long-chain acyl lysine. |
| WOS关键词 | MAMMALIAN SIRTUINS ; DEACETYLASES ; DEACYLATION ; SUBSTRATE ; INSIGHTS |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| WOS类目 | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000384807500022 |
| 出版者 | WILEY-BLACKWELL |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2375055 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Long, Yaqiu; Liu, Dongxiang |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, Dept Pharmacol 3, Beijing 100864, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Mat Med, Dept Med Chem, Beijing 100864, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Design & Dev Ctr, Beijing 100864, Peoples R China |
| 推荐引用方式 GB/T 7714 | Gai, Wei,Li, He,Jiang, Hualiang,et al. Crystal structures of sirt3 reveal that the alpha 2-alpha 3 loop and alpha 3-helix affect the interaction with long-chain acyl lysine[J]. Febs letters,2016,590(17):3019-3028. |
| APA | Gai, Wei,Li, He,Jiang, Hualiang,Long, Yaqiu,&Liu, Dongxiang.(2016).Crystal structures of sirt3 reveal that the alpha 2-alpha 3 loop and alpha 3-helix affect the interaction with long-chain acyl lysine.Febs letters,590(17),3019-3028. |
| MLA | Gai, Wei,et al."Crystal structures of sirt3 reveal that the alpha 2-alpha 3 loop and alpha 3-helix affect the interaction with long-chain acyl lysine".Febs letters 590.17(2016):3019-3028. |
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来源：中国科学院大学
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