8YU7
Cryo-EM structure of CXCR4 tetramer
Summary for 8YU7
| Entry DOI | 10.2210/pdb8yu7/pdb |
| EMDB information | 39573 |
| Descriptor | C-X-C chemokine receptor type 4, CHOLESTEROL (2 entities in total) |
| Functional Keywords | chemokine receptor, cxcr4, g protein-coupled receptor, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 166357.88 |
| Authors | |
| Primary citation | Liu, A.,Liu, Y.,Ye, R.D. Structural basis of CXCR4 assembly and regulation. Cell Rep, 44:115255-115255, 2025 Cited by PubMed Abstract: CXC chemokine receptor 4 (CXCR4) is a well-established drug target and a key representative of the chemokine receptor family. Chemokine receptors tend to assemble, and this assembly plays a critical role in regulating their functions. However, structural information regarding the organization of these receptors remains limited. Here, we present the cryoelectron microscopy (cryo-EM) structure of a CXCR4 homo-tetramer. In this tetramer, each protomer interfaces with adjacent protomers via TM1/2 and TM5/6/7, aligning at a 90° angle to assemble into a C4 rotationally symmetric arrangement. Each protomer allosterically regulates the others, with Q272 in the ECL3 loop interacting with K38 (TM1) and V99 (TM2) of the adjacent protomer, resulting in a mutually inhibitory configuration. These findings reveal an allosteric and antagonistic mechanism that prevents excessive activation, providing a structural framework for understanding the molecular mechanisms driving CXCR4 self-assembly and offering insights that could inspire further therapeutic strategies. PubMed: 39891908DOI: 10.1016/j.celrep.2025.115255 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.01 Å) |
Structure validation
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