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Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors

文献类型：期刊论文

作者Tang, Tingting7,8; Tan, Qiuxiang7; Han, Shuo7; Diemar, Anne6; Lobner, Kristin6; Wang, Hongyu5,7; Schuess, Corinna6; Behr, Victoria6; Moerl, Karin6; Wang, Mu4,7
刊名SCIENCE ADVANCES
出版日期2022-05-01
卷号8期号:18页码:14
ISSN号2375-2548
DOI10.1126/sciadv.abm1232
通讯作者Zhao, Qiang(zhaoq@simm.ac.cn) ; Wu, Beili(beiliwu@simm.ac.cn)
英文摘要In response to three highly conserved neuropeptides, neuropeptide Y (NPY), peptide YY, and pancreatic polypeptide (PP), four G protein-coupled receptors mediate multiple essential physiological processes, such as food intake, vasoconstriction, sedation, and memory retention. Here, we report the structures of the human Y-1, Y-2, and Y-4 receptors in complex with NPY or PP, and the G(i)(1) protein. These structures reveal distinct binding poses of the peptide upon coupling to different receptors, reflecting the importance of the conformational plasticity of the peptide in recognizing the NPY receptors. The N terminus of the peptide forms extensive interactions with the Y-1 receptor, but not with the Y-2 and Y-4 receptors. Supported by mutagenesis and functional studies, subtype-specific interactions between the receptors and peptides were further observed. These findings provide insight into key factors that govern NPY signal recognition and transduction, and would enable development of selective drugs.
WOS关键词NEUROPEPTIDE-Y ; PANCREATIC-POLYPEPTIDE ; FOOD-INTAKE ; BINDING ; Y-1 ; RESIDUES ; DYNAMICS ; LIGANDS ; AGONIST ; ANALOGS
资助项目National Science Foundation of China[31825010] ; National Science Foundation of China[82121005] ; National Science Foundation of China[32161133011] ; National Key R&D Program of China[2018YFA0507000] ; CAS Strategic Priority Research Program[XDB37030100] ; Shanghai Science and Technology Committee[19JC1416200] ; Shanghai Pilot Program for Basic Research-Chinese Academy of Sciences, Shanghai Branch[JCYJ-SHFY-2021-008] ; Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)[421152132] ; Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)[SFB 1423/1]
WOS研究方向Science & Technology - Other Topics
语种英语
WOS记录号WOS:000794062500006
出版者AMER ASSOC ADVANCEMENT SCIENCE
源URL[http://119.78.100.183/handle/2S10ELR8/301089]  
专题新药研究国家重点实验室
通讯作者Zhao, Qiang; Wu, Beili
作者单位1.Novo Nordisk AS, Novo Nordisk Pk, Malov, Denmark
2.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan, Peoples R China
3.Univ Regensburg, Inst Pharm, Pharmaceut Med Chem 2, Regensburg, Germany
4.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai, Peoples R China
5.Univ Chinese Acad Sci, Beijing, Peoples R China
6.Univ Leipzig, Fac Life Sci, Inst Biochem, Leipzig, Germany
7.Chinese Acad Sci, Shanghai Inst Mat Med, CAS Key Lab Receptor Res, State Key Lab Drug Res, Shanghai, Peoples R China
8.UCAS, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou, Peoples R China
推荐引用方式
GB/T 7714		 Tang, Tingting,Tan, Qiuxiang,Han, Shuo,et al. Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors[J]. SCIENCE ADVANCES,2022,8(18):14.
APA Tang, Tingting.,Tan, Qiuxiang.,Han, Shuo.,Diemar, Anne.,Lobner, Kristin.,...&Wu, Beili.(2022).Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors.SCIENCE ADVANCES,8(18),14.
MLA Tang, Tingting,et al."Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors".SCIENCE ADVANCES 8.18(2022):14.

入库方式： OAI收割

来源：上海药物研究所

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