Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.5
Classification:SIGNALING PROTEIN, HYDROLASE
Release Date:2010-10-27
Deposition Date:2010-08-11
Revision Date:2011-07-13#2012-05-02#2017-07-26
Molecular Weight:118216.37
Macromolecule Type:Protein
Residue Count:1004
Atom Site Count:7662
DOI:10.2210/pdb3odu/pdb
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.
Resolution:2.5
Classification:SIGNALING PROTEIN, HYDROLASE
Release Date:2010-10-27
Deposition Date:2010-08-11
Revision Date:2011-07-13#2012-05-02#2017-07-26
Molecular Weight:118216.37
Macromolecule Type:Protein
Residue Count:1004
Atom Site Count:7662
DOI:10.2210/pdb3odu/pdb
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.
| Date made available | 2010 |
|---|---|
| Publisher | RCSB-PDB |