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 and 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.
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.

Revision as of 00:35, 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.