Syntaxin 6 N terminal protein domain
| Syntaxin-6_N | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 syntaxin 6 | |||||||||
| Identifiers | |||||||||
| Symbol | Syntaxin-6_N | ||||||||
| Pfam | PF09177 | ||||||||
| InterPro | IPR015260 | ||||||||
| SCOP | 1lvf | ||||||||
| SUPERFAMILY | 1lvf | ||||||||
| |||||||||
In molecular biology the protein domain Syntaxin 6 N terminal protein domain is a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) found in endosomal transport vesicles. It is part of the family, of target SNAREs (t-SNAREs). It is a vital aid to exporting and importing cell cargo through a process called cell trafficking. Its SNARE motif shows significant homology to both syntaxin 1a and S25C, indicating similarity through evolutionary conservation. The structure of the syntaxin 6 N-terminal domain shows strong structural similarity with the N-terminal domains of syntaxin 1a, Sso1p, and Vam3p; despite a very low level of sequence similarity. SNARE functions essentially as a tether to hold the vesicle. The cytoplasmic regions of SNARE found on transport vesicles and target membranes interact, then a four-helix coiled coil forms. This links the cell membrane and vesicles together in such a way that it overcomes the energetic barrier to fusing two lipid bilayers. This is the way cell cargo is exchanged. This particular entry focuses on the N-terminal domain of Syntaxin 6.[1]
Structure
Members of this entry, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.[2]
Function
SNAREs play a vital role in the trafficking of cell cargo. The vesicles fuse to the cell membrane with the help of SNARE proteinds. The SNARE motifs form a four-helix bundle that contributes to the fusion of two membranes. More specifically, the N-terminal domain binds to the SNARE motif, and this intramolecular interaction decreases the rate of association with the partner SNARE. However the N terminal domain's function still remains to fully elucidated.[2]
References
- ↑ Jung JJ, Inamdar SM, Tiwari A, Choudhury A (2012). "Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6.". Biosci Rep 32 (4): 383–91. doi:10.1042/BSR20120006. PMC 3392101. PMID 22489884.
- 1 2 Misura KM, Bock JB, Gonzalez LC, Scheller RH, Weis WI (July 2002). "Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog". Proc. Natl. Acad. Sci. U.S.A. 99 (14): 9184–9. doi:10.1073/pnas.132274599. PMC 123115. PMID 12082176.
This article incorporates text from the public domain Pfam and InterPro IPR015260