Schippers, L.M. (2010) The transport mechanesm of the sodium/aspartate symporter GltPh is novel and different from LeuT. Bachelor's Thesis, Biology.
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Abstract
Re-uptake of neurotransmitters from the synaptic cleft is essential for functional neurotransmission. In recent years, some of the transporters that mediate this uptake have been crystallized and this has improved our understanding of the mechanism by which these transporters function. Two of these transporters are GltPh and LeuT, prokaryotic homologs of glutamate and leucine transporters, respectively. In eukaryotes, glutamate is an excitatory neurotransmitter and eukaryotic homologs of LeuT transport some neurotransmitters that are usually inhibitory, like GABA. These transporters are assumed to function via the alternating access mechanism, in which the substrate binding site is alternately exposed to the inside and the outside of the membrane. Several proteins from distinct families have been crystallized with a similar structure as LeuT, but in different conformations, revealing new insights in their transport mechanisms. In this review we will compare the structures and mechanisms of this LeuT-family with the structure of GltPh, that has been crystallized in only two conformations. In this way we will examine whether the structures of LeuT could be used to learn more about the transport mechanism of GltPh.
| Item Type: | Thesis (Bachelor's Thesis) |
|---|---|
| Degree programme: | Biology |
| Thesis type: | Bachelor's Thesis |
| Language: | English |
| Date Deposited: | 15 Feb 2018 07:44 |
| Last Modified: | 15 Feb 2018 07:44 |
| URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/9354 |
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