Sandbox GGC1: Difference between revisions
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== Chymotrypsin == | == Chymotrypsin == | ||
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | <StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | ||
<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. 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). | <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. 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). This study utilized a bovine pancreatic trypsin inhibitor (BTPI) in order to study the structure. | ||
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== Function == | == Function == | ||
<scene name='75/752263/Active_site/2'>The | The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. The S1 pocket is mainly hydrophobic and preferentially binds to large, nonpolar amino acids, which includes P1 tyrosine, tryptophan, and phenylalanine. <scene name='75/752263/Active_site/2'>The S1 pocket of the bovine alpha-chymotrypsin active Site is highlighed in yellow</scene> | ||
== Disease == | == Disease == | ||
