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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Functional GPCR Expression in Eukaryotic LEXSY System.

Aleksandra Luginina1, Ivan Maslov2, Polina Khorn1

  • 1Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia.

Journal of Molecular Biology
|October 8, 2023
PubMed
Summary
This summary is machine-generated.

The Leishmania tarentolae (LEXSY) eukaryotic system effectively produces G protein-coupled receptors (GPCRs) for structural studies. LEXSY offers higher yields than insect cells for producing the adenosine A2A receptor, a key drug target.

Keywords:
G protein-coupled receptorsLeishmania tarentolaeProtein biophysical characterizationRecombinant expressionSingle-molecule Förster Resonance Energy Transfer

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Area of Science:

  • Membrane protein structural biology
  • Drug discovery and development
  • Eukaryotic expression systems

Background:

  • G protein-coupled receptors (GPCRs) are a major class of drug targets, crucial for understanding cellular signaling.
  • Structural studies of GPCRs are vital for rational drug design, but large-scale recombinant production remains a significant challenge.
  • Current expression systems often face limitations in GPCR yield and stability, hindering structural determination.

Purpose of the Study:

  • To evaluate the Leishmania tarentolae (LEXSY) eukaryotic expression system for producing G protein-coupled receptors (GPCRs).
  • To compare LEXSY with established insect cell systems for GPCR production, focusing on yield, purity, and functional integrity.
  • To assess the suitability of LEXSY as a scalable platform for GPCR structural biology.

Main Methods:

  • Recombinant expression of the human adenosine A2A receptor (A2AAR) in the LEXSY eukaryotic system.
  • Purification of A2AAR from LEXSY and comparison with A2AAR produced in insect cells.
  • Characterization of purified A2AAR, including purity, stability, and ligand-induced conformational changes.

Main Results:

  • The LEXSY system demonstrated a remarkably higher protein yield for A2AAR compared to insect cell expression.
  • A2AAR purified from both systems exhibited comparable purity, stability, and exhibited similar ligand-induced conformational changes and structural dynamics.
  • LEXSY proved effective for producing a functional GPCR suitable for structural studies.

Conclusions:

  • The Leishmania tarentolae (LEXSY) eukaryotic system is a highly promising platform for the large-scale production of G protein-coupled receptors.
  • LEXSY offers significant advantages in protein yield over traditional insect cell systems for GPCR structural studies.
  • This finding supports the broader application of LEXSY in structural biology and drug discovery efforts targeting GPCRs.