Introduction of SNAPG

N-ethylmaleimide-sensitive factor (NSF) attachment protein, gamma or SNAP-gamma is a member of a family related soluble NSF attachment proteins. SNAP-gamma protein structure obtained from Danio rerio organism comprises of 4 identical molecular chains (Chain A, B, C and D) interacting to one another via non-bonded contacts. Each chain is 307 amino acid residues in length and made of 69% helical secondary structure of 16 helices, 34 helix-helix interaction, 8 beta turns and 2 gamma turns[1]. Two types of molecular component were observed to formed interactions with SNAPG molecule. These molecular components were sulfanate ion(SO4) and selenomethionine (MSE)(Figure 1). The sulfanate ions interact differently to different residues of different chain, unlike MSE in which included into SNAPG amino acid sequences as modified residue (Figure 2.B,C & 3).

SNAP-gamma is located on chromosome 18, location 18p11.22. This protein belongs to the SNAP family and can be found on the cellular compartment; membrane and peripheral membrane protein (by similarity). Its roles within eukaryotic cells have not been discussed widely compared to SNAP-alpha or SNAP-beta. However it is believed that SNAP-gamma is required for fusion of lipid bilayers thus promoting vesicular transport in membrane trafficking such as endocytosis and exocytosis. Some articles stated that the existence of distinct alpha/beta-SNAP and gamma-SNAP-binding sites in Golgi membranes that appear to be part of the same receptor complex. SNAP-gamma was also appeared to be conserved in many sequences of various organisms both prokaryotic but not in eukaryotic lineages. We have been conducted a further experiment to predict SNAP-gamma structure, function and evolution using several internet databases and available softwares. This report would show how its structure, function and evolutionary were predicted by comparing its protein sequences to known protein, and later looked at what the output is.

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