Inward-Facing Conformation of Glutamate Transporters as Revealed by Their Inverted-Topology Structur...
Inward-Facing Conformation of Glutamate Transporters as Revealed by Their Inverted-Topology Structural Repeats
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United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
Glutamate transporters regulate synaptic concentrations of this neurotransmitter by coupling its flux to that of sodium and other cations. Available crystal structures of an archeal homologue of these transporters, GltPh, resemble an extracellular-facing state, in which the bound substrate is occluded only by a small helical hairpin segment called...
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Full title
Inward-Facing Conformation of Glutamate Transporters as Revealed by Their Inverted-Topology Structural Repeats
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TN_cdi_proquest_miscellaneous_748960652
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_748960652
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.0908570106
