EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Constitutive activation mechanism of a class C GPCR.
ジャーナル・号・ページ	Nat Struct Mol Biol, Vol. 31, Issue 4, Page 678-687, Year 2024
掲載日	2024年2月8日
著者	Jinwoo Shin / Junhyeon Park / Jieun Jeong / Jordy Homing Lam / Xingyu Qiu / Di Wu / Kuglae Kim / Joo-Youn Lee / Carol V Robinson / Jaekyung Hyun / Vsevolod Katritch / Kwang Pyo Kim / Yunje Cho /
PubMed 要旨	Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a ...Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a class C orphan GPCR, is unique because it lacks an ECD and exhibits constitutive activity. Impaired GPR156-G signaling contributes to loss of hearing. Here we present the cryo-electron microscopy structures of human GPR156 in the G-free and G-coupled states. We found that an endogenous phospholipid molecule is located within each TMD of the GPR156 dimer. Asymmetric binding of Gα to the phospholipid-bound GPR156 dimer restructures the first and second intracellular loops and the carboxy-terminal part of the elongated transmembrane 7 (TM7) without altering dimer conformation. Our findings reveal that GPR156 is a transducer for phospholipid signaling. Constant binding of abundant phospholipid molecules and the G-protein-induced reshaping of the cytoplasmic face provide a basis for the constitutive activation of GPR156.
リンク	Nat Struct Mol Biol / PubMed:38332368
手法	EM (単粒子)
解像度	2.61 - 3.33 Å
構造データ	35377 8ieb EMDB-35377, PDB-8ieb: Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine) 手法: EM (単粒子) / 解像度: 3.03 Å 35378 8iec EMDB-35378, PDB-8iec: Cryo-EM structure of miniGo-scFv16 of GPR156-miniGo-scFv16 complex (local refine) 手法: EM (単粒子) / 解像度: 3.18 Å 35380 8ied EMDB-35380, PDB-8ied: Cryo-EM structure of GPR156-miniGo-scFv16 complex 手法: EM (単粒子) / 解像度: 3.33 Å 35382 8iei EMDB-35382, PDB-8iei: Cryo-EM structure of GPR156A/B of G-protein free GPR156 (local refine) 手法: EM (単粒子) / 解像度: 2.62 Å 35389 8iep EMDB-35389, PDB-8iep: Cryo-EM structure of GPR156C/D of G-protein free GPR156 (local refine) 手法: EM (単粒子) / 解像度: 2.61 Å 35390 8ieq EMDB-35390, PDB-8ieq: Cryo-EM structure of G-protein free GPR156 手法: EM (単粒子) / 解像度: 2.73 Å
化合物	PDB-1lya: CRYSTAL STRUCTURES OF NATIVE AND INHIBITED FORMS OF HUMAN CATHEPSIN D: IMPLICATIONS FOR LYSOSOMAL TARGETING AND DRUG DESIGN
由来	homo sapiens (ヒト) mus musculus (ハツカネズミ)
キーワード	SIGNALING PROTEIN / Membrane protein / G-protein coupled receptor / Signal transduction / Phospholipid