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TitleIdentification and mechanism of G protein-biased ligands for chemokine receptor CCR1.
Journal, issue, pagesNat Chem Biol, Vol. 18, Issue 3, Page 264-271, Year 2022
Publish dateDec 23, 2021
AuthorsZhehua Shao / Qingya Shen / Bingpeng Yao / Chunyou Mao / Li-Nan Chen / Huibing Zhang / Dan-Dan Shen / Chao Zhang / Weijie Li / Xufei Du / Fei Li / Honglei Ma / Zhi-Hua Chen / H Eric Xu / Songmin Ying / Yan Zhang / Huahao Shen /
PubMed AbstractBiased signaling of G protein-coupled receptors describes an ability of different ligands that preferentially activate an alternative downstream signaling pathway. In this work, we identified and ...Biased signaling of G protein-coupled receptors describes an ability of different ligands that preferentially activate an alternative downstream signaling pathway. In this work, we identified and characterized different N-terminal truncations of endogenous chemokine CCL15 as balanced or biased agonists targeting CCR1, and presented three cryogenic-electron microscopy structures of the CCR1-G complex in the ligand-free form or bound to different CCL15 truncations with a resolution of 2.6-2.9 Å, illustrating the structural basis of natural biased signaling that initiates an inflammation response. Complemented with pharmacological and computational studies, these structures revealed it was the conformational change of Tyr291 (Y291) in CCR1 that triggered its polar network rearrangement in the orthosteric binding pocket and allosterically regulated the activation of β-arrestin signaling. Our structure of CCL15-bound CCR1 also exhibited a critical site for ligand binding distinct from many other chemokine-receptor complexes, providing new insights into the mode of chemokine recognition.
External linksNat Chem Biol / PubMed:34949837 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 2.9 Å
Structure data

32020

7vl8

EMDB-32020, PDB-7vl8:
Cryo-EM structure of the Apo CCR1-Gi complex
Method: EM (single particle) / Resolution: 2.9 Å

32021

7vl9

EMDB-32021, PDB-7vl9:
Cryo-EM structure of the CCL15(26-92) bound CCR1-Gi complex
Method: EM (single particle) / Resolution: 2.6 Å

32022

7vla

EMDB-32022, PDB-7vla:
Cryo-EM structure of the CCL15(27-92) bound CCR1-Gi complex
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR / CCR1 / Chemokine Receptor / MEMBRNE PROTEIN

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