7F1R

Cryo-EM structure of the chemokine receptor CCR5 in complex with RANTES and Gi

Summary for 7F1R

• Entry DOI: 10.2210/pdb7f1r/pdb
• EMDB information: 31423
• Descriptor: C-C motif chemokine 5,C-C chemokine receptor type 5, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (4 entities in total)
• Functional Keywords: g protein-coupled receptor, chemokine receptor ccr5, rantes, signaling protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 137826.44

Authors

Zhang, H.,Chen, K.,Tan, Q.,Han, S.,Zhu, Y.,Zhao, Q.,Wu, B. (deposition date: 2021-06-09, release date: 2021-07-14, Last modification date: 2024-10-23)

Primary citation

Zhang, H.,Chen, K.,Tan, Q.,Shao, Q.,Han, S.,Zhang, C.,Yi, C.,Chu, X.,Zhu, Y.,Xu, Y.,Zhao, Q.,Wu, B.
Structural basis for chemokine recognition and receptor activation of chemokine receptor CCR5.
Nat Commun, 12:4151-4151, 2021

PubMed Abstract: 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.

PubMed: 34230484
DOI: 10.1038/s41467-021-24438-5

Experimental method

ELECTRON MICROSCOPY (3 Å)