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Shao, Zhehua; Tan, Yangxia; Shen, Qingya; Hou, Li; Yao, Bingpeng; Qin, Jiao; Xu, Peiyu; Mao, Chunyou; Chen, Li-Nan; Zhang, Huibing; Shen, Dan-Dan; Zhang, Chao; Li, Weijie; Du, Xufei; Li, Fei; Chen, Zhi-Hua; Jiang, Yi; Xu, H Eric; Ying, Songmin; Ma, Honglei; Zhang, Yan; Shen, Huahao
Cell discovery, 05/2022, Volume: 8, Issue: 1Journal Article
Chemokine receptors are a family of G-protein-coupled receptors with key roles in leukocyte migration and inflammatory responses. Here, we present cryo-electron microscopy structures of two human CC chemokine receptor-G-protein complexes: CCR2 bound to its endogenous ligand CCL2, and CCR3 in the apo state. The structure of the CCL2-CCR2-G-protein complex reveals that CCL2 inserts deeply into the extracellular half of the transmembrane domain, and forms substantial interactions with the receptor through the most N-terminal glutamine. Extensive hydrophobic and polar interactions are present between both two chemokine receptors and the Gα-protein, contributing to the constitutive activity of these receptors. Notably, complemented with functional experiments, the interactions around intracellular loop 2 of the receptors are found to be conserved and play a more critical role in G-protein activation than those around intracellular loop 3. Together, our findings provide structural insights into chemokine recognition and receptor activation, shedding lights on drug design targeting chemokine receptors.
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