Structure, Dynamics and Activation Mechanisms of Chemokine Receptors:


A hybrid structural approach to analyze ligand binding by the serotonin type 4 receptor (5-HT4)

Structure, Dynamics and Activation Mechanisms of Chemokine Receptors

Hybrid structural methods have been used in recent years to understand protein-protein or protein-ligand interactions where high resolution crystallography or NMR data on the protein of interest has been limited. Here, we used structural mass spectrometry along with theoretical computations, modeling, and other biochemical methods to develop a structured model for human serotonin receptor subtype 4(b) in the presence and absence of its antagonist GR125487. Overall, this study reveals the potential of hybrid structural methods, including mass spectrometry, to probe physiological and functional GPCR-ligand interactions with purified native protein.

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A novel approach to quantify G-protein-coupled receptor dimerization equilibrium using bioluminescence resonance energy transfer

Structure, Dynamics and Activation Mechanisms of Chemokine Receptors

Bioluminescence resonance energy transfer (BRET) has been used to quantify protein-protein interactions in the cell. The utility of this method is demonstrated by its application to the homodimerization of WT and mutant forms of the chemokine receptor CXCR4.

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