2. Academic Validation
  3. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists

Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists

  • Science. 2010 Nov 19;330(6007):1066-71. doi: 10.1126/science.1194396.
Beili Wu 1,  Ellen Y T Chien,  Clifford D Mol,  Gustavo Fenalti,  Wei Liu,  Vsevolod Katritch,  Ruben Abagyan,  Alexei Brooun,  Peter Wells,  F Christopher Bi,  Damon J Hamel,  Peter Kuhn,  Tracy M Handel,  Vadim Cherezov,  Raymond C Stevens
Affiliations

Affiliation

  • 1 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
PMID: 20929726 DOI: 10.1126/science.1194396
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.

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