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Updated: Feb 10, 2026
08:49
Cell Surface Receptor Identification Using Genome-Scale CRISPR/Cas9 Genetic Screens
Published on: June 6, 2020
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CCR5 adopts three homodimeric conformations that control cell surface delivery.
Jun Jin1,2, Fanny Momboisse1, Gaelle Boncompain3
1Institut National de la Santé et de la Recherche Médicale Unit 1108, Viral Pathogenesis Unit, Department of Virology, Institut Pasteur, 75015 Paris, France.
Science Signaling
|May 10, 2018
Summary
Chemokine receptor CCR5 forms distinct dimers, crucial for HIV-1 co-receptor function and cell surface targeting. Maraviroc binding stabilizes a specific dimeric state, offering new inhibition strategies.
Area of Science:
- Structural biology
- Virology
- Molecular pharmacology
Background:
- Class A G protein-coupled receptors (GPCRs) are known to form homodimers.
- CCR5 is a critical co-receptor for HIV-1 entry into host cells.
Purpose of the Study:
- To characterize the dimerization interfaces of the chemokine receptor CCR5.
- To investigate the role of CCR5 dimerization in receptor function and HIV-1 entry.
Main Methods:
- Computational approaches
- Receptor cross-linking
- Energy transfer assays
- Functional export assays
Main Results:
- Identified three distinct dimeric organizations of CCR5 involving transmembrane helix 5.
- Two dimeric states were observed in unliganded CCR5, with maraviroc stabilizing a third state.
- CCR5 dimerization is essential for its proper targeting to the plasma membrane.
Conclusions:
- CCR5 dimerization contributes to the conformational diversity of inactive class A GPCRs.
- Understanding CCR5 dimerization offers new avenues for investigating HIV-1 cellular entry and developing novel inhibition strategies.
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