Sandbox 46
From Proteopedia
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<applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | ||
| + | =Trypsin= | ||
| + | Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site. such, it contains a serine residue in the active site. | ||
| - | = Structure= | + | ==Structure== |
To follow the primary structure (amino acid sequence) of Trypsin, click <scene name='Sandbox_46/Secondary_structure_tryp/2'>here.</scene> The N-terminus is blue and the C-terminus is red. | To follow the primary structure (amino acid sequence) of Trypsin, click <scene name='Sandbox_46/Secondary_structure_tryp/2'>here.</scene> The N-terminus is blue and the C-terminus is red. | ||
Revision as of 01:51, 29 October 2010
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Trypsin
Trypsin, a member of the serine protease family, is produced in the pancreas and found in the digestive tracks of vertebrates. To avoid pancreatic self-degradation, trypsin is synthesized as trypsinogen, a zymogen. Cleavage by enteropeptidase allows tryspin to enter its active form. As a serine protease, trypsin contains a serine residue in its active site. such, it contains a serine residue in the active site.
Structure
To follow the primary structure (amino acid sequence) of Trypsin, click The N-terminus is blue and the C-terminus is red.
The of Trypsin consists of two alpha helices (light green) and two beta sheets (peach). The yellow and red molecules are not part of the Trypsin structure; they were added during crystallization to freeze Trypsin in a specific conformation. Fix THIS. they bind at active site
Shared active site
