Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling
Formylpeptide receptors (FPRs) are a class of chemotactic G protein-coupled receptors (GPCRs) that recognize pathogen- and host-derived formylpeptides. Here the authors report the 3.17 Å cryo-EM structure of the human FPR2-Gi signaling complex with a bound peptide agonist and in combination with com...
Guardado en:
Autores principales: | , , , , , , , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/3c877c5e058b47a68a52db49730981f1 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:3c877c5e058b47a68a52db49730981f1 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:3c877c5e058b47a68a52db49730981f12021-12-02T17:32:59ZStructure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling10.1038/s41467-020-14728-92041-1723https://doaj.org/article/3c877c5e058b47a68a52db49730981f12020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14728-9https://doaj.org/toc/2041-1723Formylpeptide receptors (FPRs) are a class of chemotactic G protein-coupled receptors (GPCRs) that recognize pathogen- and host-derived formylpeptides. Here the authors report the 3.17 Å cryo-EM structure of the human FPR2-Gi signaling complex with a bound peptide agonist and in combination with computational docking and MD simulations provide mechanistic insights into formylpeptide recognition by FPRs.Youwen ZhuangHeng LiuX. Edward ZhouRavi Kumar VermaParker W. de WaalWonjo JangTing-Hai XuLei WangXing MengGongpu ZhaoYanyong KangKarsten MelcherHao FanNevin A. LambertH. Eric XuCheng ZhangNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Youwen Zhuang Heng Liu X. Edward Zhou Ravi Kumar Verma Parker W. de Waal Wonjo Jang Ting-Hai Xu Lei Wang Xing Meng Gongpu Zhao Yanyong Kang Karsten Melcher Hao Fan Nevin A. Lambert H. Eric Xu Cheng Zhang Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
description |
Formylpeptide receptors (FPRs) are a class of chemotactic G protein-coupled receptors (GPCRs) that recognize pathogen- and host-derived formylpeptides. Here the authors report the 3.17 Å cryo-EM structure of the human FPR2-Gi signaling complex with a bound peptide agonist and in combination with computational docking and MD simulations provide mechanistic insights into formylpeptide recognition by FPRs. |
format |
article |
author |
Youwen Zhuang Heng Liu X. Edward Zhou Ravi Kumar Verma Parker W. de Waal Wonjo Jang Ting-Hai Xu Lei Wang Xing Meng Gongpu Zhao Yanyong Kang Karsten Melcher Hao Fan Nevin A. Lambert H. Eric Xu Cheng Zhang |
author_facet |
Youwen Zhuang Heng Liu X. Edward Zhou Ravi Kumar Verma Parker W. de Waal Wonjo Jang Ting-Hai Xu Lei Wang Xing Meng Gongpu Zhao Yanyong Kang Karsten Melcher Hao Fan Nevin A. Lambert H. Eric Xu Cheng Zhang |
author_sort |
Youwen Zhuang |
title |
Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
title_short |
Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
title_full |
Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
title_fullStr |
Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
title_full_unstemmed |
Structure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signaling |
title_sort |
structure of formylpeptide receptor 2-gi complex reveals insights into ligand recognition and signaling |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/3c877c5e058b47a68a52db49730981f1 |
work_keys_str_mv |
AT youwenzhuang structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT hengliu structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT xedwardzhou structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT ravikumarverma structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT parkerwdewaal structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT wonjojang structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT tinghaixu structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT leiwang structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT xingmeng structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT gongpuzhao structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT yanyongkang structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT karstenmelcher structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT haofan structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT nevinalambert structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT hericxu structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling AT chengzhang structureofformylpeptidereceptor2gicomplexrevealsinsightsintoligandrecognitionandsignaling |
_version_ |
1718380113971642368 |