Dataset on Galanin Receptor 3 mutants that improve recombinant receptor expression and stability in an agonist and antagonist bound form

• Published in: Data in brief 2017-06, Vol.12 (C), p.603-607
• Main Authors: Ho, Thao T., Nguyen, Jasmine T., Liu, Juping, Stanczak, Pawel, Thompson, Aaron A., Yan, Yingzhuo G., Chen, Jasmine, Allerston, Charles K., Dillard, Charles L., Xu, Hao, Shoger, Nicholas J., Cameron, Jill S., Massari, Mark E., Aertgeerts, Kathleen
• Format: Article
• Language: English
• Subjects: Data; Galanin Receptor type 3; GPCR protein stabilization; GPCR recombinant protein expression; Membrane protein; Protein engineering; Virus-like particles
• ISSN: 2352-3409; 2352-3409
• DOI: 10.1016/j.dib.2017.04.057

Galanin Receptor 3 (GALR3) is a G-protein-coupled receptor with a widespread distribution in the brain and plays a role in a variety of physiologic processes including cognition/memory, sensory/pain processing, hormone secretion, and feeding behavior. Therefore, GALR3 is considered an attractive CNS drug target (Freimann et al., 2015) [1]. This dataset contains GALR3 point mutants that improve recombinant protein expression and thermal stability of the receptor contained in virus-like particles (VLPs) or obtained by detergent-purification of baculovirus-infected insect cells. The mutations listed can be grouped in those that improve the stability of the agonist-bound and the antagonist-bound form of the receptor. Protein characteristics in terms of protein expression and thermal stability were comparable between GPCR-VLP and GPCR overexpressing Sf9 cultures. The further analysis and detailed results of these mutants as well as their impact on biophysical assay development for drug discovery can be found in “Method for Rapid Optimization of Recombinant GPCR Protein Expression and Stability using Virus-Like Particles” (Ho et al., 2017) [2].