Study of two G-protein coupled receptor variants of human trace amine-associated receptor 5.

Scientific Reports
Xiaoqiang WangShuguang Zhang

Abstract

Here we report the study of two bioengineered variants of human trace amine-associated receptor 5 (hTAAR5) that were expressed in stable tetracycline-inducible HEK293S cell lines. A systematic detergent screen showed that fos-choline-14 was the optimal detergent to solubilize and subsequently purify the receptors. Milligram quantities of both hTAAR5 variants were purified to near homogeneity using immunoaffinity chromatography followed by gel filtration. Circular dichroism showed that the purified receptors had helical secondary structures, indicating that they were properly folded. The purified receptors are not only suitable for functional analyses, but also for subsequent crystallization trials. To our knowledge, this is the first mammalian TAAR that has been heterologously expressed and purified. Our study will likely stimulate in the development of therapeutic drug targets for TAAR-associated diseases, as well as fabrication of TAAR-based sensing devices.

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Citations

Nov 5, 2016·Archives of Biochemistry and Biophysics·Dinesh K YadavNarendra Tuteja
Jun 27, 2018·Pharmacological Reviews·Raul R GainetdinovMark D Berry
Jan 11, 2014·Applied Biochemistry and Biotechnology·Xiaoqiang WangJiqian Wang
Sep 27, 2018·Scientific Reports·Valentin M SluchDennis S Rice
Sep 18, 2020·Protein Science : a Publication of the Protein Society·Shuguang Zhang

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Methods Mentioned

BETA
dot blot
gel filtration
Circular dichroism
glycosylation
dot blots

Software Mentioned

Aviv

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