Analysis of conformational changes of a G protein-coupled receptor that are propagated to a novel intracellular factor.

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We succeeded in constructing a protein expression system for a novel intracellular factor FROUNT that regulates a chemokine receptor CCR2b using Escherichia coli cells and developing a protocol for the protein purification. Utilizing this system and protocol, we obtained large amounts of purified full-length FROUNT proteins that are enough for structural analyses. We elucidated that the purified FROUNT proteins possess CCR2b-binding activity with solution NMR and surface plasmon resonance. We also succeeded in constructing a protein expression system of full-length CCR2b using insect cells and developing a protocol for the protein purification.