X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release
Neurotransmitter:sodium symporters (NSS) serve as targets for drugs including antidepressants and psychostimulants. Here authors report the X-ray structure of the prokaryotic NSS member, LeuT, in a Na+/substrate-bound, inward-facing occluded conformation which is a key intermediate in the LeuT trans...
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Nature Portfolio
2020
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oai:doaj.org-article:b7943f31d4e74b9daf78fc8c7d1b60c12021-12-02T15:39:18ZX-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release10.1038/s41467-020-14735-w2041-1723https://doaj.org/article/b7943f31d4e74b9daf78fc8c7d1b60c12020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14735-whttps://doaj.org/toc/2041-1723Neurotransmitter:sodium symporters (NSS) serve as targets for drugs including antidepressants and psychostimulants. Here authors report the X-ray structure of the prokaryotic NSS member, LeuT, in a Na+/substrate-bound, inward-facing occluded conformation which is a key intermediate in the LeuT transport cycle.Kamil GotfrydThomas BoesenJonas S. MortensenGeorge KhelashviliMatthias QuickDaniel S. TerryJulie W. MisselMichael V. LeVinePontus GourdonScott C. BlanchardJonathan A. JavitchHarel WeinsteinClaus J. LolandPoul NissenUlrik GetherNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020) |
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Science Q Kamil Gotfryd Thomas Boesen Jonas S. Mortensen George Khelashvili Matthias Quick Daniel S. Terry Julie W. Missel Michael V. LeVine Pontus Gourdon Scott C. Blanchard Jonathan A. Javitch Harel Weinstein Claus J. Loland Poul Nissen Ulrik Gether X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
description |
Neurotransmitter:sodium symporters (NSS) serve as targets for drugs including antidepressants and psychostimulants. Here authors report the X-ray structure of the prokaryotic NSS member, LeuT, in a Na+/substrate-bound, inward-facing occluded conformation which is a key intermediate in the LeuT transport cycle. |
format |
article |
author |
Kamil Gotfryd Thomas Boesen Jonas S. Mortensen George Khelashvili Matthias Quick Daniel S. Terry Julie W. Missel Michael V. LeVine Pontus Gourdon Scott C. Blanchard Jonathan A. Javitch Harel Weinstein Claus J. Loland Poul Nissen Ulrik Gether |
author_facet |
Kamil Gotfryd Thomas Boesen Jonas S. Mortensen George Khelashvili Matthias Quick Daniel S. Terry Julie W. Missel Michael V. LeVine Pontus Gourdon Scott C. Blanchard Jonathan A. Javitch Harel Weinstein Claus J. Loland Poul Nissen Ulrik Gether |
author_sort |
Kamil Gotfryd |
title |
X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
title_short |
X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
title_full |
X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
title_fullStr |
X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
title_full_unstemmed |
X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release |
title_sort |
x-ray structure of leut in an inward-facing occluded conformation reveals mechanism of substrate release |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/b7943f31d4e74b9daf78fc8c7d1b60c1 |
work_keys_str_mv |
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