8WRB

Lysophosphatidylserine receptor GPR34-Gi complex

8WRB の概要

• エントリーDOI: 10.2210/pdb8wrb/pdb
• EMDBエントリー: 37771
• 分子名称: Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (8 entities in total)
• 機能のキーワード: complex, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 182209.48

構造登録者

Gong, W.,Liu, G.,Li, X.,Wang, Y.,Zhang, X. (登録日: 2023-10-13, 公開日: 2023-11-08, 最終更新日: 2024-11-20)

主引用文献

Liu, G.,Li, X.,Wang, Y.,Zhang, X.,Gong, W.
Structural basis for ligand recognition and signaling of the lysophosphatidylserine receptors GPR34 and GPR174.
Plos Biol., 21:e3002387-e3002387, 2023

PubMed Abstract: Lysophosphatidylserine (LysoPS) is a naturally occurring lipid mediator involved in various physiological and pathological processes especially those related to the immune system. GPR34, GPR174, and P2Y10 have been identified as the receptors for LysoPS, and its analogues have been developed as agonists or antagonists for these receptors. However, the lack of structural information hinders the drug development with novel characteristics, such as nonlipid ligands and allosteric modulators. Here, we determined the structures of human GPR34 and GPR174 in complex with LysoPS and G protein by cryo-EM. Combined with structural analysis and functional studies, we elucidated the lipid-binding modes of these receptors. By structural comparison, we identified the structural features of GPR34 and GPR174 in active state. Taken together, our findings provide insights into ligand recognition and signaling of LysoPS receptors and will facilitate the development of novel therapeutics for related inflammatory diseases and autoimmune diseases.

PubMed: 38048360
DOI: 10.1371/journal.pbio.3002387

実験手法

ELECTRON MICROSCOPY (2.91 Å)