Sandbox GGC1
From Proteopedia
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<scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref> | <scene name='75/752263/Intro/1'>Chymotrypsin</scene> is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure of bovine α-chymotrypsin homodimer.<ref>PMID:15544809</ref> | ||
| - | == Function == | + | == Structural Highlights and Function == |
| - | The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. | + | Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). The active site of chymotrypsin consists of a <scene name='75/752263/Active_site/3'>catalytic triad</scene> (Ser 195, His 57, Asp 102), which are highlighted in blue. |
The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow. | The S1 binding pocket is responsible for stabilization of the substrate in the active site prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes tyrosine, tryptophan, and phenylalanine. The <scene name='75/752263/Active_site/2'>S1 pocket</scene> of the bovine α-chymotrypsin is highlighted in yellow. | ||
Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. | Chymotrypsin and other serine protease enzymes catalyzes the cleavage of amino acids. Both the active site and S1 pocket can be seen <scene name='75/752263/Both_active_site_and_s1/1'>here</scene>. The catalytic triad is highlighted in blue and the S1 pocket is highlighted in yellow. | ||
<scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene> | <scene name='75/752263/S1_pocket_active_site/1'>Text To Be Displayed</scene> | ||
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| - | == Structural highlights == | ||
| - | Chymotrypsin is composed of <scene name='75/752263/Three_chains/2'>three chains</scene> (residues 1-13 shown in maroon, 16-146 shown in blue, and 149-245 shown in gold). | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 02:26, 28 April 2017
Chymotrypsin
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References
- ↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088
