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-Structure paper
タイトル | Structural insights into the agonists binding and receptor selectivity of human histamine H receptor. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 6538, Year 2023 |
掲載日 | 2023年10月20日 |
著者 | Dohyun Im / Jun-Ichi Kishikawa / Yuki Shiimura / Hiromi Hisano / Akane Ito / Yoko Fujita-Fujiharu / Yukihiko Sugita / Takeshi Noda / Takayuki Kato / Hidetsugu Asada / So Iwata / |
PubMed 要旨 | Histamine is a biogenic amine that participates in allergic and inflammatory processes by stimulating histamine receptors. The histamine H receptor (HR) is a potential therapeutic target for chronic ...Histamine is a biogenic amine that participates in allergic and inflammatory processes by stimulating histamine receptors. The histamine H receptor (HR) is a potential therapeutic target for chronic inflammatory diseases such as asthma and atopic dermatitis. Here, we show the cryo-electron microscopy structures of the HR-G complex bound with an endogenous agonist histamine or the selective agonist imetit bound in the orthosteric binding pocket. The structures demonstrate binding mode of histamine agonists and that the subtype-selective agonist binding causes conformational changes in Phe344, which, in turn, form the "aromatic slot". The results provide insights into the molecular underpinnings of the agonism of HR and subtype selectivity of histamine receptors, and show that the HR structures may be valuable in rational drug design of drugs targeting the HR. |
リンク | Nat Commun / PubMed:37863901 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 - 3.1 Å |
構造データ | EMDB-33785, PDB-7yfc: EMDB-33786, PDB-7yfd: |
化合物 | ChemComp-HSM: ChemComp-CLR: ChemComp-ITF: |
由来 |
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キーワード | MEMBRANE PROTEIN / GPCR / Aminergic receptor / Histamine receptor |