Sandbox wabash15

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=="Structure of Trypsin"==
=="Structure of Trypsin"==
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By: Luke Knutson and Graham Redweik
This is a sub structure of trypsin '''Sandbox wabash15'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
This is a sub structure of trypsin '''Sandbox wabash15'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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<StructureSection load='2agg' size='340' side='right' caption='Acyl intermediate of trypsin catalyzed hydrolysis=''>
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*'''Trypsin''' is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered. Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.
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*'''Trypsin''' is a serine protease formed in the small intestine and catalyzes the hydrolysis of smaller peptides. As with other members of its family, it possesses a <scene name='Sandbox_45/Ctriadd102h57s195/4'>catalytic triad</scene> (His-57, Asp-102, and Ser-195). This active site produces a nucleophilicity that enables its reaction with the serine groups on its substrate, i.e. smaller peptides. Within the catalytic triad-active site, an oxyanion hole exists that essentially stabilizes the acyl-intermediate states of the reaction, creating a binding pocket for the reaction to take place. These acyl-intermediates are key in protease reactions, as they are very susceptible to hydrolysis reactions, providing an opportunity for the second substrate of trypsin (water) to hydrolyze the interaction between His-57 and the attached C-terminus end of the protein substrate.. To stabilize this process, Asp-189 stabilizes the reaction by mediating an interaction with Lys or other positively-charged residues on the smaller protein.
== Function ==
== Function ==

Current revision

"Structure of Trypsin"

By: Luke Knutson and Graham Redweik This is a sub structure of trypsin Sandbox wabash15. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

PDB ID 2agg

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