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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| Language: | English |
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Nature Publishing Group
2020-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-14735-w |
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doaj-b7943f31d4e74b9daf78fc8c7d1b60c12021-05-11T08:40:40ZengNature Publishing GroupNature Communications2041-17232020-02-0111111410.1038/s41467-020-14735-wX-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate releaseKamil Gotfryd0Thomas Boesen1Jonas S. Mortensen2George Khelashvili3Matthias Quick4Daniel S. Terry5Julie W. Missel6Michael V. LeVine7Pontus Gourdon8Scott C. Blanchard9Jonathan A. Javitch10Harel Weinstein11Claus J. Loland12Poul Nissen13Ulrik Gether14Molecular Neuropharmacology and Genetics Laboratory, Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenDANDRITE - Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus UniversityMolecular Neuropharmacology and Genetics Laboratory, Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenDepartment of Physiology and Biophysics, Weill Cornell Medical College, Cornell UniversityDepartment of Psychiatry, Columbia University Vagelos College of Physicians & Surgeon and Division of Molecular Therapeutics, New York State Psychiatric InstituteDepartment of Structural Biology, St. Jude Children’s Research HospitalMembrane Protein Structural Biology Group, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of CopenhagenDepartment of Physiology and Biophysics, Weill Cornell Medical College, Cornell UniversityMembrane Protein Structural Biology Group, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of CopenhagenDepartment of Structural Biology, St. Jude Children’s Research HospitalDepartment of Psychiatry, Columbia University Vagelos College of Physicians & Surgeon and Division of Molecular Therapeutics, New York State Psychiatric InstituteDepartment of Physiology and Biophysics, Weill Cornell Medical College, Cornell UniversityMolecular Neuropharmacology and Genetics Laboratory, Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenDANDRITE - Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus UniversityMolecular Neuropharmacology and Genetics Laboratory, Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenNeurotransmitter: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.https://doi.org/10.1038/s41467-020-14735-w |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| 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 |
| spellingShingle |
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 Nature Communications |
| 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 Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2020-02-01 |
| 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. |
| url |
https://doi.org/10.1038/s41467-020-14735-w |
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