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@ARTICLE{Sharma:810932,
author = {Sharma, Kanika and Ahuja, Gaurav and Hussain, Ashiq and
Balfanz, Sabine and Baumann, A. and Korsching, Sigrun I.},
title = {{E}limination of a ligand gating site generates a
supersensitive olfactory receptor},
journal = {Scientific reports},
volume = {6},
issn = {2045-2322},
address = {London},
publisher = {Nature Publishing Group},
reportid = {FZJ-2016-03498},
pages = {28359},
year = {2016},
abstract = {Olfaction poses one of the most complex ligand-receptor
matching problems in biology due to the unparalleled
multitude of odor molecules facing a large number of cognate
olfactory receptors. We have recently deorphanized an
olfactory receptor, TAAR13c, as a specific receptor for the
death-associated odor cadaverine. Here we have modeled the
cadaverine/TAAR13c interaction, exchanged predicted binding
residues by site-directed mutagenesis, and measured the
activity of the mutant receptors. Unexpectedly we observed a
binding site for cadaverine at the external surface of the
receptor, in addition to an internal binding site, whose
mutation resulted in complete loss of activity. In stark
contrast, elimination of the external binding site generated
supersensitive receptors. Modeling suggests this site to act
as a gate, limiting access of the ligand to the internal
binding site and thereby downregulating the affinity of the
native receptor. This constitutes a novel mechanism to
fine-tune physiological sensitivity to socially relevant
odors.},
cin = {ICS-4},
ddc = {000},
cid = {I:(DE-Juel1)ICS-4-20110106},
pnm = {552 - Engineering Cell Function (POF3-552)},
pid = {G:(DE-HGF)POF3-552},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000378197600001},
pubmed = {pmid:27323929},
doi = {10.1038/srep28359},
url = {https://juser.fz-juelich.de/record/810932},
}