Taste substance binding elicits conformational change of taste receptor T1r heterodimer extracellular domains View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-09

AUTHORS

Eriko Nango, Shuji Akiyama, Saori Maki-Yonekura, Yuji Ashikawa, Yuko Kusakabe, Elena Krayukhina, Takahiro Maruno, Susumu Uchiyama, Nipawan Nuemket, Koji Yonekura, Madoka Shimizu, Nanako Atsumi, Norihisa Yasui, Takaaki Hikima, Masaki Yamamoto, Yuji Kobayashi, Atsuko Yamashita

ABSTRACT

Sweet and umami tastes are perceived by T1r taste receptors in oral cavity. T1rs are class C G-protein coupled receptors (GPCRs), and the extracellular ligand binding domains (LBDs) of T1r1/T1r3 and T1r2/T1r3 heterodimers are responsible for binding of chemical substances eliciting umami or sweet taste. However, molecular analyses of T1r have been hampered due to the difficulties in recombinant expression and protein purification, and thus little is known about mechanisms for taste perception. Here we show the first molecular view of reception of a taste substance by a taste receptor, where the binding of the taste substance elicits a different conformational state of T1r2/T1r3 LBD heterodimer. Electron microscopy has showed a characteristic dimeric structure. Förster resonance energy transfer and X-ray solution scattering have revealed the transition of the dimerization manner of the ligand binding domains, from a widely spread to compactly organized state upon taste substance binding, which may correspond to distinct receptor functional states. More... »

PAGES

25745

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep25745

DOI

http://dx.doi.org/10.1038/srep25745

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044778067

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27160511


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