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Logo of jbcThe Journal of Biological Chemistry
J Biol Chem. 2015 February 13; 290(7): 3893.
PMCID: PMC4326799

Digging into the Finer Details of the Structures and Functions of G Protein-coupled Receptors ♦

Single Molecule Analysis of Functionally Asymmetric G Protein-coupled Receptor (GPCR) Oligomers Reveals Diverse Spatial and Structural Assemblies

♦ See referenced article, J. Biol. Chem. 2015, 290, 3875–3892

G protein-coupled receptors (GPCRs) are complex proteins that can associate as dimers and oligomers to carry out the GPCR signaling function. However, researchers don't understand the details of how the individual receptors function within the larger GPCR complex. In this Paper of the Week, a team led by Aylin Hanyaloglu and Ilpo Huhtaniemi at Imperial College London carried out the imaging of individual GPCRs at an 8-nm resolution. The proteins they studied were stripped-down versions of a natural GPCR, the luteinizing hormone receptor. The functional dimers and oligomers of the receptor were seen to have particular spatial geometries. Changing the asymmetry of the receptor oligomer changed its signaling sensitivity and strength. The investigators also carried out structural modeling that integrated the super-resolution imaging and identified a surprising diversity in the interfaces that were necessary for oligomer formation. They say, “The combination of super-resolution imaging with structural modeling provides an unprecedented molecular insight into the complexity and spatial and structural signatures mediating GPCR oligomerization.”

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Visualizing individual GPCR oligomers with both super-resolution imaging (i) and molecular modeling (ii) unveils the complexity and diversity in di/oligomer interfaces.

Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology