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Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
Beili Wu1, Ellen Y T Chien, Clifford D Mol
1Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Abstract:
Chemokine receptors are critical regulators of cell migration in the context of immune surveillance, inflammation, and development. The G protein-coupled chemokine receptor CXCR4 is specifically implicated in cancer metastasis and HIV-1 infection. Here we report five independent crystal structures of CXCR4 bound to an antagonist small molecule IT1t and a cyclic peptide CVX15 at 2.5 to 3.2 angstrom resolution. All structures reveal a consistent homodimer with an interface including helices V and VI that may be involved in regulating signaling. The location and shape of the ligand-binding sites differ from other G protein-coupled receptors and are closer to the extracellular surface. These structures provide new clues about the interactions between CXCR4 and its natural ligand CXCL12, and with the HIV-1 glycoprotein gp120.
Insights
Structural insights into the chemokine receptor CXCR4 reveal a homodimer crucial for cell migration. These findings impact understanding of cancer metastasis and HIV-1 infection.
Area of Science:
- Structural Biology
- Molecular Biology
- Immunology
Background:
- Chemokine receptors, such as CXCR4, regulate immune cell migration.
- CXCR4 is implicated in cancer metastasis and HIV-1 infection.
Purpose of the Study:
- To determine the crystal structures of CXCR4 bound to antagonists.
- To elucidate the structural basis of CXCR4 function and ligand interactions.
Main Methods:
- X-ray crystallography
- Structure determination at 2.5 to 3.2 angstrom resolution.
- Analysis of CXCR4-ligand complexes.
Main Results:
- Five crystal structures of CXCR4 with antagonists IT1t and CVX15 were determined.
- A consistent homodimer interface involving helices V and VI was observed.
- CXCR4 ligand-binding sites are distinct from other GPCRs and located near the extracellular surface.
Conclusions:
- The identified CXCR4 homodimer may regulate receptor signaling.
- Structural data provides insights into CXCR4 interactions with CXCL12 and HIV-1 gp120.
- These findings offer a basis for developing novel therapeutics targeting CXCR4.
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