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Structure and function analyses of the purified GPCR human vomeronasal type 1 receptor 1.


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(50) approximately 1 µM. This expression system can enable structural and functional analyses towards understanding how mammalian scent detection works.

SUBMITTER: Corin K 

PROVIDER: S-EPMC3240957 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Structure and function analyses of the purified GPCR human vomeronasal type 1 receptor 1.

Corin Karolina K   Baaske Philipp P   Geissler Sandra S   Wienken Christoph J CJ   Duhr Stefan S   Braun Dieter D   Zhang Shuguang S  

Scientific reports 20111128


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  ...[more]

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