Structural basis of ligand binding modes at the human formyl peptide receptor 2

Formyl peptide receptors (FPRs) are GPCRs that play important roles in transducing chemotactic signals in phagocytes and mediating host-defense and inflammatory responses. Here the authors present the 2.8 Å crystal structure of human FPR2 in complex with the peptide agonist WKYMVm and in combination...

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Autores principales:	Tong Chen, Muya Xiong, Xin Zong, Yunjun Ge, Hui Zhang, Mu Wang, Gye Won Han, Cuiying Yi, Limin Ma, Richard D. Ye, Yechun Xu, Qiang Zhao, Beili Wu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6a6c3a3f8432461e92e7060e4f1bd1bd
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spelling	oai:doaj.org-article:6a6c3a3f8432461e92e7060e4f1bd1bd2021-12-02T17:33:13ZStructural basis of ligand binding modes at the human formyl peptide receptor 210.1038/s41467-020-15009-12041-1723https://doaj.org/article/6a6c3a3f8432461e92e7060e4f1bd1bd2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15009-1https://doaj.org/toc/2041-1723Formyl peptide receptors (FPRs) are GPCRs that play important roles in transducing chemotactic signals in phagocytes and mediating host-defense and inflammatory responses. Here the authors present the 2.8 Å crystal structure of human FPR2 in complex with the peptide agonist WKYMVm and in combination with molecular docking, ligand-binding and signalling assays provide further insights into the binding modes of FPR2 to both non-formyl and formyl peptides.Tong ChenMuya XiongXin ZongYunjun GeHui ZhangMu WangGye Won HanCuiying YiLimin MaRichard D. YeYechun XuQiang ZhaoBeili WuNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tong Chen Muya Xiong Xin Zong Yunjun Ge Hui Zhang Mu Wang Gye Won Han Cuiying Yi Limin Ma Richard D. Ye Yechun Xu Qiang Zhao Beili Wu Structural basis of ligand binding modes at the human formyl peptide receptor 2
description	Formyl peptide receptors (FPRs) are GPCRs that play important roles in transducing chemotactic signals in phagocytes and mediating host-defense and inflammatory responses. Here the authors present the 2.8 Å crystal structure of human FPR2 in complex with the peptide agonist WKYMVm and in combination with molecular docking, ligand-binding and signalling assays provide further insights into the binding modes of FPR2 to both non-formyl and formyl peptides.
format	article
author	Tong Chen Muya Xiong Xin Zong Yunjun Ge Hui Zhang Mu Wang Gye Won Han Cuiying Yi Limin Ma Richard D. Ye Yechun Xu Qiang Zhao Beili Wu
author_facet	Tong Chen Muya Xiong Xin Zong Yunjun Ge Hui Zhang Mu Wang Gye Won Han Cuiying Yi Limin Ma Richard D. Ye Yechun Xu Qiang Zhao Beili Wu
author_sort	Tong Chen
title	Structural basis of ligand binding modes at the human formyl peptide receptor 2
title_short	Structural basis of ligand binding modes at the human formyl peptide receptor 2
title_full	Structural basis of ligand binding modes at the human formyl peptide receptor 2
title_fullStr	Structural basis of ligand binding modes at the human formyl peptide receptor 2
title_full_unstemmed	Structural basis of ligand binding modes at the human formyl peptide receptor 2
title_sort	structural basis of ligand binding modes at the human formyl peptide receptor 2
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/6a6c3a3f8432461e92e7060e4f1bd1bd
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Structural basis of ligand binding modes at the human formyl peptide receptor 2

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