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TitleCryo-EM Structure and Biochemical Analysis of the Human Chemokine Receptor CCR8.
Journal, issue, pagesBiochemistry, Vol. 63, Issue 15, Page 1892-1900, Year 2024
Publish dateAug 6, 2024
AuthorsQi Peng / Haihai Jiang / Xinyu Cheng / Na Wang / Sili Zhou / Yuting Zhang / Tingting Yang / Yixiang Chen / Wei Zhang / Sijia Lv / Weiwei Nan / JianFei Wang / Guo-Huang Fan / Jian Li / Jin Zhang /
PubMed AbstractThe C-C motif chemokine receptor 8 (CCR8) is a class A G-protein-coupled receptor that has emerged as a promising therapeutic target in cancer and autoimmune diseases. In the present study, we solved ...The C-C motif chemokine receptor 8 (CCR8) is a class A G-protein-coupled receptor that has emerged as a promising therapeutic target in cancer and autoimmune diseases. In the present study, we solved the cryo-electron microscopy (cryo-EM) structure of the human CCR8-G complex in the absence of a ligand at 2.58 Å. Structural analysis and comparison revealed that our apo CCR8 structure undergoes some conformational changes and is similar to that in the CCL1-CCR8 complex structure, indicating an active state. In addition, the key residues of CCR8 involved in the recognition of LMD-009, a potent nonpeptide agonist, were investigated by mutating CCR8 and testing the calcium flux induced by LMD-009-CCR8 interaction. Three mutants of CCR8, Y113A, Y172A, and E286A, showed a dramatically decreased ability in mediating calcium mobilization, indicating their key interaction with LMD-009 and key roles in activation. These structural and biochemical analyses enrich molecular insights into the agonism and activation of CCR8 and will facilitate CCR8-targeted therapy.
External linksBiochemistry / PubMed:38985857
MethodsEM (single particle)
Resolution2.58 Å
Structure data

38481

8xml

EMDB-38481, PDB-8xml:
Cryo-EM structure of the Apo CCR8-Gi complex
Method: EM (single particle) / Resolution: 2.58 Å

Source
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsSTRUCTURAL PROTEIN / Cryo-EM / CCR8 / GPCR

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