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  1. Article ; Online: Structural insights into the peptide selectivity and activation of human neuromedin U receptors

    Chongzhao You / Yumu Zhang / Peiyu Xu / Sijie Huang / Wanchao Yin / H. Eric Xu / Yi Jiang

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 10

    Abstract: Neuromedin U receptors (NMURs) are potential drug targets for obesity and inflammatory disorders. Here, the authors report structural basis for neuromedin recognition and activation mechanism of NMURs. ...

    Abstract Neuromedin U receptors (NMURs) are potential drug targets for obesity and inflammatory disorders. Here, the authors report structural basis for neuromedin recognition and activation mechanism of NMURs.
    Keywords Science ; Q
    Language English
    Publishing date 2022-04-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Author Correction

    Heng Liu / Qing Zhang / Xinheng He / Mengting Jiang / Siwei Wang / Xiaoci Yan / Xi Cheng / Yang Liu / Fa-Jun Nan / H. Eric Xu / Xin Xie / Wanchao Yin

    Nature Communications, Vol 14, Iss 1, Pp 1-

    Structural insights into ligand recognition and activation of the medium-chain fatty acid-sensing receptor GPR84

    2023  Volume 1

    Keywords Science ; Q
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Structural insights into ligand recognition and activation of the medium-chain fatty acid-sensing receptor GPR84

    Heng Liu / Qing Zhang / Xinheng He / Mengting Jiang / Siwei Wang / Xiaoci Yan / Xi Cheng / Yang Liu / Fa-Jun Nan / H. Eric Xu / Xin Xie / Wanchao Yin

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Volume 14

    Abstract: Abstract GPR84 is an orphan class A G protein-coupled receptor (GPCR) that is predominantly expressed in immune cells and plays important roles in inflammation, fibrosis, and metabolism. Here, we present cryo-electron microscopy (cryo-EM) structures of ... ...

    Abstract Abstract GPR84 is an orphan class A G protein-coupled receptor (GPCR) that is predominantly expressed in immune cells and plays important roles in inflammation, fibrosis, and metabolism. Here, we present cryo-electron microscopy (cryo-EM) structures of Gαi protein-coupled human GPR84 bound to a synthetic lipid-mimetic ligand, LY237, or a putative endogenous ligand, a medium-chain fatty acid (MCFA) 3-hydroxy lauric acid (3-OH-C12). Analysis of these two ligand-bound structures reveals a unique hydrophobic nonane tail -contacting patch, which forms a blocking wall to select MCFA-like agonists with the correct length. We also identify the structural features in GPR84 that coordinate the polar ends of LY237 and 3-OH-C12, including the interactions with the positively charged side chain of R172 and the downward movement of the extracellular loop 2 (ECL2). Together with molecular dynamics simulations and functional data, our structures reveal that ECL2 not only contributes to direct ligand binding, but also plays a pivotal role in ligand entry from the extracellular milieu. These insights into the structure and function of GPR84 could improve our understanding of ligand recognition, receptor activation, and Gαi-coupling of GPR84. Our structures could also facilitate rational drug discovery against inflammation and metabolic disorders targeting GPR84.
    Keywords Science ; Q
    Subject code 612
    Language English
    Publishing date 2023-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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    Inter-library loan at ZB MED

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  4. Article ; Online: Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor

    Yue Wang / Shimeng Guo / Youwen Zhuang / Ying Yun / Peiyu Xu / Xinheng He / Jia Guo / Wanchao Yin / H. Eric Xu / Xin Xie / Yi Jiang

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 9

    Abstract: Ghrelin is a gastric peptide hormone and its acylation is required for binding to and activation of the ghrelin receptor in the brain, which initiates appetite. Here, the authors present cryo-EM structures of the Gq-coupled ghrelin receptor bound to ... ...

    Abstract Ghrelin is a gastric peptide hormone and its acylation is required for binding to and activation of the ghrelin receptor in the brain, which initiates appetite. Here, the authors present cryo-EM structures of the Gq-coupled ghrelin receptor bound to ghrelin and the synthetic agonist GHRP-6 and they describe how the acylated peptide hormone is recognised by the receptor, which is of interest for drug design.
    Keywords Science ; Q
    Language English
    Publishing date 2021-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Molecular basis for allosteric agonism and G protein subtype selectivity of galanin receptors

    Jia Duan / Dan-Dan Shen / Tingting Zhao / Shimeng Guo / Xinheng He / Wanchao Yin / Peiyu Xu / Yujie Ji / Li-Nan Chen / Jinyu Liu / Huibing Zhang / Qiufeng Liu / Yi Shi / Xi Cheng / Hualiang Jiang / H. Eric Xu / Yan Zhang / Xin Xie / Yi Jiang

    Nature Communications, Vol 13, Iss 1, Pp 1-

    2022  Volume 13

    Abstract: The basis for the diverse peptide-binding modes and the G protein selectivity of peptide GPCRs remains elusive. Here, the authors offer a structural basis for allosteric-like agonism and G protein selectivity of a neuropeptide GPCR, galanin receptor. ...

    Abstract The basis for the diverse peptide-binding modes and the G protein selectivity of peptide GPCRs remains elusive. Here, the authors offer a structural basis for allosteric-like agonism and G protein selectivity of a neuropeptide GPCR, galanin receptor.
    Keywords Science ; Q
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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