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TitleStructural insights into endogenous ligand selectivity and activation mechanisms of FFAR1 and FFAR2.
Journal, issue, pagesCell Rep, Vol. 43, Issue 12, Page 115024, Year 2024
Publish dateNov 30, 2024
AuthorsYudun Ke / Yimiao Huang / Cuiying Yi / Limin Ma / Xiaojing Chu / Beili Wu / Qiang Zhao / Shuo Han /
PubMed AbstractFree fatty acid receptors (FFARs) play critical roles in metabolic regulation and are potential therapeutic targets for metabolic and inflammatory diseases. A comprehensive understanding of the ...Free fatty acid receptors (FFARs) play critical roles in metabolic regulation and are potential therapeutic targets for metabolic and inflammatory diseases. A comprehensive understanding of the activation mechanisms and endogenous ligand selectivity of FFARs is essential for drug discovery. Here, we report two cryoelectron microscopy structures of the human FFAR1 bound to the endogenous ligand docosahexaenoic acid (DHA) and G protein as well as FFAR2 in complex with butyrate and G at 3.2 Å and 3.3 Å resolution, respectively. These structures highlight that distinct locations and sizes of the orthosteric ligand binding pockets are crucial determinants of the endogenous ligand selectivity of this receptor subfamily. Additionally, computational analysis reveals a potential allosteric ligand binding pocket in FFAR2. Furthermore, we observe that the upward movement of helix V upon endogenous ligand binding is responsible for receptor activation. These insights will significantly aid in the development of drugs targeting this receptor family.
External linksCell Rep / PubMed:39616615
MethodsEM (single particle)
Resolution3.2 - 3.34 Å
Structure data

61971

9k1c

EMDB-61971, PDB-9k1c:
Cryo-EM structure of the DHA bound FFA1-Gi complex
Method: EM (single particle) / Resolution: 3.2 Å

61972

9k1d

EMDB-61972, PDB-9k1d:
Cryo-EM structure of the butyrate bound FFA2-Gi complex
Method: EM (single particle) / Resolution: 3.34 Å

Chemicals

ChemComp-HXA:
DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID

ChemComp-BUA:
butanoic acid

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR / FFAR1

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