Abstract of SNAPG: Difference between revisions
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Soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) has three different form of isoforms; alpha-,beta- and gamma-. The SNAP family can be found on the cellular compartment; membrane and peripheral membrane protein. The SNAP-gamma functions are still under investigations unlike the other two isoforms. Structure-based alignment with vesicular transport protein sec17 in yeast has shown many similar physical properties suggesting that these proteins may also have similar interaction pattern with ligands and/or other proteins. However, SNAP-gamma and sec17 sequence alignment was problematic as it was difficult to acquire optimal alignment for conserved active site investigations. | Soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) has three different form of isoforms; alpha-,beta- and gamma-. The SNAP family can be found on the cellular compartment; membrane and peripheral membrane protein. The SNAP-gamma functions are still under investigations unlike the other two isoforms. Structure-based alignment with vesicular transport protein sec17 in yeast has shown many similar physical properties suggesting that these proteins may also have similar interaction pattern with ligands and/or other proteins. However, SNAP-gamma and sec17 sequence alignment was problematic as it was difficult to acquire optimal alignment for conserved active site investigations. According to phylogenetic tree analysis, SNAP-gamma (SNAPG) Protein evolved in almost all eukaryotes family. Thus it was concluded that SNAPG protein is an important protein in Eukaryotes organism. There is no SNAPG protein detected in prokaryotes organism. | ||
Latest revision as of 01:18, 12 June 2007
Soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) has three different form of isoforms; alpha-,beta- and gamma-. The SNAP family can be found on the cellular compartment; membrane and peripheral membrane protein. The SNAP-gamma functions are still under investigations unlike the other two isoforms. Structure-based alignment with vesicular transport protein sec17 in yeast has shown many similar physical properties suggesting that these proteins may also have similar interaction pattern with ligands and/or other proteins. However, SNAP-gamma and sec17 sequence alignment was problematic as it was difficult to acquire optimal alignment for conserved active site investigations. According to phylogenetic tree analysis, SNAP-gamma (SNAPG) Protein evolved in almost all eukaryotes family. Thus it was concluded that SNAPG protein is an important protein in Eukaryotes organism. There is no SNAPG protein detected in prokaryotes organism.
