Sandbox 46
From Proteopedia
| Line 1: | Line 1: | ||
<applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Trypsin' /> | ||
=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. | + | 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. |
==Structure== | ==Structure== | ||
| Line 16: | Line 16: | ||
<scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | <scene name='Sandbox_46/Polar_vs_nonpolar_wire/1'>Wire</scene> | ||
| - | + | ==Stability== | |
<scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | <scene name='Sandbox_46/Disulfide_bonds/3'>Disulfide</scene> | ||
<scene name='Sandbox_46/Disulfide_bonds_123/1'>DS bonds labeled</scene> | <scene name='Sandbox_46/Disulfide_bonds_123/1'>DS bonds labeled</scene> | ||
| + | |||
| + | <scene name='Sandbox_46/Hbonds_backbone/1'>H bonds backbone</scene> | ||
| + | |||
| + | <scene name='Sandbox_46/H_bonds_r_groups/1'>H bonds r groups</scene> | ||
| + | |||
| + | ==Function== | ||
| + | |||
<scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | <scene name='Sandbox_46/Ac1/1'>Active Site 1</scene> | ||
| Line 30: | Line 37: | ||
<scene name='Sandbox_46/Ac_all/1'>All active sites</scene> '''Shared active site''' | <scene name='Sandbox_46/Ac_all/1'>All active sites</scene> '''Shared active site''' | ||
| - | |||
| - | <scene name='Sandbox_46/Hbonds_backbone/1'>H bonds backbone</scene> | ||
| - | |||
| - | <scene name='Sandbox_46/H_bonds_r_groups/1'>H bonds r groups</scene> | ||
Revision as of 01:54, 29 October 2010
|
Contents |
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.
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
Stability
Function
Shared active site
