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TitleStructural basis for chemokine recognition and receptor activation of chemokine receptor CCR5.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4151, Year 2021
Publish dateJul 6, 2021
AuthorsHui Zhang / Kun Chen / Qiuxiang Tan / Qiang Shao / Shuo Han / Chenhui Zhang / Cuiying Yi / Xiaojing Chu / Ya Zhu / Yechun Xu / Qiang Zhao / Beili Wu /
PubMed AbstractThe chemokine receptor CCR5 plays a vital role in immune surveillance and inflammation. However, molecular details that govern its endogenous chemokine recognition and receptor activation remain ...The chemokine receptor CCR5 plays a vital role in immune surveillance and inflammation. However, molecular details that govern its endogenous chemokine recognition and receptor activation remain elusive. Here we report three cryo-electron microscopy structures of G protein-coupled CCR5 in a ligand-free state and in complex with the chemokine MIP-1α or RANTES, as well as the crystal structure of MIP-1α-bound CCR5. These structures reveal distinct binding modes of the two chemokines and a specific accommodate pattern of the chemokine for the distal N terminus of CCR5. Together with functional data, the structures demonstrate that chemokine-induced rearrangement of toggle switch and plasticity of the receptor extracellular region are critical for receptor activation, while a conserved tryptophan residue in helix II acts as a trigger of receptor constitutive activation.
External linksNat Commun / PubMed:34230484 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 3.0 Å
Structure data

31422

7f1q

EMDB-31422, PDB-7f1q:
Cryo-EM structure of the chemokine receptor CCR5 in complex with MIP-1a and Gi
Method: EM (single particle) / Resolution: 2.9 Å

31423

7f1r

EMDB-31423, PDB-7f1r:
Cryo-EM structure of the chemokine receptor CCR5 in complex with RANTES and Gi
Method: EM (single particle) / Resolution: 3.0 Å

31424

7f1s

EMDB-31424, PDB-7f1s:
Cryo-EM structure of the apo chemokine receptor CCR5 in complex with Gi
Method: EM (single particle) / Resolution: 2.8 Å

PDB-7f1t:
Crystal structure of the human chemokine receptor CCR5 in complex with MIP-1a
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • clostridium pasteurianum (bacteria)
KeywordsSIGNALING PROTEIN / G Protein-coupled receptor / Chemokine Receptor CCR5 / MIP-1a / RANTES / G protein

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