Biology:Sodium:dicarboxylate symporter

From HandWiki
Short description: Protein family
SDF
PDB 2nwx EBI.jpg
crystal structure of gltph in complex with l-aspartate and sodium ions
Identifiers
SymbolSDF
PfamPF00375
InterProIPR001991
PROSITEPDOC00591
TCDB2.A.23
OPM superfamily20
OPM protein2nwl

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

  1. "A functional superfamily of sodium/solute symporters". Biochim. Biophys. Acta 1197 (2): 133–66. June 1994. doi:10.1016/0304-4157(94)90003-5. PMID 8031825. 
  2. "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. November 1992. doi:10.1073/pnas.89.22.10955. PMID 1279699. Bibcode1992PNAS...8910955S. 
  3. "Cloning and expression of a rat brain L-glutamate transporter". Nature 360 (6403): 464–7. December 1992. doi:10.1038/360464a0. PMID 1448170. Bibcode1992Natur.360..464P. 
  4. "Primary structure and functional characterization of a high-affinity glutamate transporter". Nature 360 (6403): 467–71. December 1992. doi:10.1038/360467a0. PMID 1280334. Bibcode1992Natur.360..467K. 
This article incorporates text from the public domain Pfam and InterPro: IPR001991