Sodium:dicarboxylate symporter

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SDF
crystal structure of gltph in complex with l-aspartate and sodium ions
Identifiers
SymbolSDF
PfamPF00375
InterProIPR001991
PROSITEPDOC00591
TCDB2.A.23
OPM superfamily20
OPM protein2nwl
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

It has been shown [1] that integral membrane proteins that mediate the uptake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. One of these families [2] is known as the sodium:dicarboxylate symporter family (SDF) (it is different from divalent anion–sodium symporter).

Such re-uptake of neurotransmitters from the synapses, is thought to be an important mechanism for terminating their action, by removing these chemicals from the synaptic cleft, and transporting them into presynaptic nerve terminals, and surrounding neuroglia. this removal is also believed to prevent them accumulating to the point of reaching neurotoxic.[3][4]

The structure of these transporter proteins has been variously reported to contain from 8 to 10 transmembrane (TM) regions, although 10 now seems to be the accepted value.

Members of the family include: several mammalian excitatory amino acid transporters, and a number of bacterial transporters. They vary with regards to their dependence on transport of sodium, and other ions.

References[edit]

  1. ^ Reizer J, Reizer A, Saier MH (June 1994). "A functional superfamily of sodium/solute symporters". Biochim. Biophys. Acta. 1197 (2): 133–66. doi:10.1016/0304-4157(94)90003-5. PMID 8031825.
  2. ^ Storck T, Schulte S, Hofmann K, Stoffel W (November 1992). "Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain". Proc. Natl. Acad. Sci. U.S.A. 89 (22): 10955–9. Bibcode:1992PNAS...8910955S. doi:10.1073/pnas.89.22.10955. PMC 50461. PMID 1279699.
  3. ^ Pines G, Danbolt NC, Bjørås M, Zhang Y, Bendahan A, Eide L, Koepsell H, Storm-Mathisen J, Seeberg E, Kanner BI (December 1992). "Cloning and expression of a rat brain L-glutamate transporter". Nature. 360 (6403): 464–7. Bibcode:1992Natur.360..464P. doi:10.1038/360464a0. PMID 1448170. S2CID 4243369.
  4. ^ Kanai Y, Hediger MA (December 1992). "Primary structure and functional characterization of a high-affinity glutamate transporter". Nature. 360 (6403): 467–71. Bibcode:1992Natur.360..467K. doi:10.1038/360467a0. PMID 1280334. S2CID 2199229.
This article incorporates text from the public domain Pfam and InterPro: IPR001991