Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori
文献类型：期刊论文
| 作者 | Shen, Zhangfei2; Jiang, Xue2; Yan, Lili3; Chen, Yu3; Wang, Weiwei3; Shi, Ying3; Shi, Liangen2; Liu, Dongxiang1 ; Zhou, Naiming3
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| 刊名 | FASEB JOURNAL
 |
| 出版日期 | 2018-03 |
| 卷号 | 32期号:3页码:1338-1353 |
| 关键词 | GPCR neuropeptide signaling structure-activity relationship |
| ISSN号 | 0892-6638 |
| DOI | 10.1096/fj.201700931R |
| 文献子类 | Article |
| 英文摘要 | Diapause hormone (DH) is a 24-aa amidated neuropeptide that elicits the embryonic diapause of the silkworm, Bombyx mori (Bommo), via sensitive and selective interaction with its receptor, Bommo DH receptor (Bommo-DHR). Previous studies of the structure-activity relationship of Bommo-DH were all based on an in vivo diapause-induction bioassay, which has provided little information on the structure of Bommo-DHR or its iteration with DH. Here, to unveil the interaction of Bommo-DH with its receptor, N-terminally truncated analogs and alanine-scanning mutants of Bommo-DH were chemically synthesized and functionally evaluated by using a Cy5.5-labeled Bommo-DH competitive binding assay and Bommo-DHR-based functional assays, including cAMP assay and Ca2+ mobilization assay. Our study demonstrates that the C-terminal residues of Arg23 and Leu24 of Bommo-DH are essential for the binding and activation of Bommo-DHR, and that Trp19 and Phe20 also contribute to the functional activity of Bommo-DH. In contrast, when Gly21 or Pro22 were replaced with alanine, both mutants exhibited binding and signaling activities that were indistinguishable from the wild-type peptide. Furthermore, our homology modeling and molecular dynamics simulations, together with experimental validations, have identified the residues of Glu89, Phe172, Phe194, and Tyr299 in Bommo-DHR that are critically involved in the interaction with Bommo-DH. These results may deepen our understanding of the interactions of class-AGPCRs with their peptidic ligands, particularly those between pheromone biosynthesis-activating neuropeptide/DH family neuropeptides and their cognate receptors.-Shen, Z., Jiang, X., Yan, L., Chen, Y., Wang, W., Shi, Y., Shi, L., Liu, D., Zhou, N. Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori. |
| WOS关键词 | PROTEIN-COUPLED RECEPTOR ; NEUROPEPTIDE FAMILY ; BIOLOGICAL-ACTIVITY ; EMBRYONIC DIAPAUSE ; IDENTIFICATION ; INSECT ; COEVOLUTION ; ACTIVATION ; INDUCTION ; PEPTIDES |
| 资助项目 | National Natural Science Foundation of China[31272375] ; National Natural Science Foundation of China[31572462] ; National Natural Science Foundation of China[21472206] ; National Natural Science Foundation of China[21672233] ; Science and Technology Project of Zhejiang, China[2016C32079] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000427246000018 |
| 出版者 | FEDERATION AMER SOC EXP BIOL |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/279871]  |
| 专题 | 药理学第三研究室 |
| 通讯作者 | Liu, Dongxiang; Zhou, Naiming |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Mat Med, Dept Pharmacol 3, Shanghai 201203, Peoples R China 2.Zhejiang Univ, Coll Anim Sci, Dept Econ Zool, Hangzhou, Zhejiang, Peoples R China; 3.Zhejiang Univ, Coll Life Sci, Inst Biochem, Zijingang Campus, Hangzhou 310058, Zhejiang, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Shen, Zhangfei,Jiang, Xue,Yan, Lili,et al. Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori[J]. FASEB JOURNAL,2018,32(3):1338-1353. |
| APA | Shen, Zhangfei.,Jiang, Xue.,Yan, Lili.,Chen, Yu.,Wang, Weiwei.,...&Zhou, Naiming.(2018).Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori.FASEB JOURNAL,32(3),1338-1353. |
| MLA | Shen, Zhangfei,et al."Structural basis for the interaction of diapause hormone with its receptor in the silkworm, Bombyx mori".FASEB JOURNAL 32.3(2018):1338-1353. |
入库方式： OAI收割
来源：上海药物研究所
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