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, Wei3,4; Li, He2,4; Jiang, Hualiang1,4 ; Long, Yaqiu2,4; Liu, Dongxiang3,4
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| 刊名 | FEBS LETTERS
 |
| 出版日期 | 2016-09 |
| 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 |
| 文献子类 | Article |
| 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 |
| 资助项目 | National Natural Science Foundation of China[21472206] ; National Natural Science Foundation of China[21672233] ; CAS Key Laboratory of Receptor Research[00000000] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000384807500022 |
| 出版者 | WILEY-BLACKWELL |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/275909]  |
| 专题 | 药理学第三研究室 |
| 通讯作者 | Long, Yaqiu; Liu, Dongxiang |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Design & Dev Ctr, Beijing 100864, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Mat Med, Dept Med Chem, Beijing 100864, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Mat Med, Key Lab Receptor Res, Dept Pharmacol 3, Beijing 100864, Peoples R China; 4.Univ Chinese Acad Sci, Beijing, 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. |
入库方式： OAI收割
来源：上海药物研究所
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