Structure and function analyses of the purified GPCR human vomeronasal type 1 receptor 1
Name
Corin-2011-Structure and function.pdf
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Author(s)
Corin, Karolina A.
Baaske, Philipp
Geissler, Sandra
Wienken, Christoph J.
Duhr, Stefan
Braun, Dieter
Zhang, Shuguang
Date Issued
November 2011
Journal
Scientific Reports
Publisher
Nature Publishing Group
Citation
Corin, Karolina, Philipp Baaske, Sandra Geissler, Christoph J. Wienken, Stefan Duhr, Dieter Braun, and Shuguang Zhang. “Structure and Function Analyses of the Purified GPCR Human Vomeronasal Type 1 Receptor 1.” Sci. Rep. 1 (November 28, 2011).
Version
Final published version
Abstract
The vomeronasal system is one of several fine-tuned scent-detecting signaling systems in mammals. However, despite significant efforts, how these receptors detect scent remains an enigma. One reason is the lack of sufficient purified receptors to perform detailed biochemical, biophysical and structural analyses. Here we report the ability to express and purify milligrams of purified, functional human vomeronasal receptor hVN1R1. Circular dichroism showed that purified hVN1R1 had an alpha-helical structure, similar to that of other GPCRs. Microscale thermophoresis showed that hVN1R1 bound its known ligand myrtenal with an EC[subscript 50] ∼1 µM. This expression system can enable structural and functional analyses towards understanding how mammalian scent detection works.
MIT Department
Massachusetts Institute of Technology. Center for Biomedical Engineering
Massachusetts Institute of Technology. Media Laboratory
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DOI of Published Version
https://doi.org/10.1038/srep00172
