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TitleStructural basis of CXCR4 assembly and regulation.
Journal, issue, pagesCell Rep, Vol. 44, Issue 2, Page 115255, Year 2025
Publish dateFeb 25, 2025
AuthorsAijun Liu / Yezhou Liu / Richard D Ye /
PubMed AbstractCXC 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 ...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.
External linksCell Rep / PubMed:39891908
MethodsEM (single particle)
Resolution3.01 Å
Structure data

39573

8yu7

EMDB-39573, PDB-8yu7:
Cryo-EM structure of CXCR4 tetramer
Method: EM (single particle) / Resolution: 3.01 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Chemokine receptor / CXCR4 / G protein-coupled receptor

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