7F1T

Crystal structure of the human chemokine receptor CCR5 in complex with MIP-1a

7F1T の概要

• エントリーDOI: 10.2210/pdb7f1t/pdb
• 分子名称: C-C motif chemokine 3,C-C chemokine receptor type 5,Rubredoxin,C-C chemokine receptor type 5, ZINC ION (2 entities in total)
• 機能のキーワード: g protein-coupled receptor, chemokine receptor ccr5, mip-1a, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55510.86

構造登録者

Zhang, H.,Chen, K.,Tan, Q.,Han, S.,Zhu, Y.,Zhao, Q.,Wu, B. (登録日: 2021-06-09, 公開日: 2021-07-14, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)