Sandbox 30: Difference between revisions
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<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
= Trypsin = | = '''Trypsin''' = | ||
[[Image:1qlq.jpg|left|200px]] | |||
(Specifically PDB: 1QLQ) | (Specifically PDB: 1QLQ) | ||
==Overview | ==Overview== | ||
Trypsin was first isolated by Wilhelm Kühne in 1867<ref>[https://www.doria.fi/bitstream/handle/10024/2142/trypsinr.pdf?sequence=1 ISBN 952-10-1863-1]</ref>. Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated. This prevents trypsin from digesting actual body tissue<ref> [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGT-49S6WV8-1&_user=4187488&_coverDate=12/31/2003&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000062504&_version=1&_urlVersion=0&_userid=4187488&md5=a7d7e1b154a43b709d5228c4852e5d10&searchtype=a doi:10.1016/j.theochem.2003.08.072]</ref>. Serine proteases were instrumental in the discovery and subsequent study of enzymes due to there high stability and large quantities in digestive juices. One of the first proteins to be studied via X-ray crystallography was Chymotrypsin. Trypsin cleaves on the C-terminus side of lysine and arginine<ref>[http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb46_1.html Protein Data Bank]</ref>. | Trypsin was first isolated by Wilhelm Kühne in 1867<ref>[https://www.doria.fi/bitstream/handle/10024/2142/trypsinr.pdf?sequence=1 ISBN 952-10-1863-1]</ref>. Trypsin is a serine protease synthesized in the pancreas but is not activated until the zymogen form of trypsin is activated. This prevents trypsin from digesting actual body tissue<ref> [http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TGT-49S6WV8-1&_user=4187488&_coverDate=12/31/2003&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000062504&_version=1&_urlVersion=0&_userid=4187488&md5=a7d7e1b154a43b709d5228c4852e5d10&searchtype=a doi:10.1016/j.theochem.2003.08.072]</ref>. Serine proteases were instrumental in the discovery and subsequent study of enzymes due to there high stability and large quantities in digestive juices. One of the first proteins to be studied via X-ray crystallography was Chymotrypsin. Trypsin cleaves on the C-terminus side of lysine and arginine<ref>[http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb46_1.html Protein Data Bank]</ref>. | ||
An easy way to distinguish between main structural components of the protein is to view it using <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration.</scene> | An easy way to distinguish between main structural components of the protein is to view it using <scene name='Sandbox_30/Trypsin_cartoon_rainbow/2'>rainbow coloration.</scene> | ||
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[[Image:SO4_Ligand.JPG|right|200px]] | [[Image:SO4_Ligand.JPG|right|200px]] | ||
===Ligands=== | |||
There are four <scene name='Sandbox_30/So4_ligands/1'>ligands</scene> present in 1QLQ, which are stabilized mostly by hydrogen bonding. For example, <scene name='Sandbox_30/So4_ligand_62_a/1'>SO4 62 A</scene> is stabilized by hydrogen bonds using the oxygens on SO4. There is a image to the right showing the bonding interaction. | There are four <scene name='Sandbox_30/So4_ligands/1'>ligands</scene> present in 1QLQ, which are stabilized mostly by hydrogen bonding. For example, <scene name='Sandbox_30/So4_ligand_62_a/1'>SO4 62 A</scene> is stabilized by hydrogen bonds using the oxygens on SO4. There is a image to the right showing the bonding interaction. | ||
==Other Relevant Information== | |||
Trypsin's zymogen form is called trypsinogen, and can actually activate itself. Zymogens require a biochemical change to activate. Only an activated form of trypsin can activate the trypsinogen, and this initial activation is carried out by enteropeptidase, which is a serine protease as well. Because activated forms of trypsin can activate others, trypsin is said to be autocatalytic<ref>Voet, Donald et al. Fundamentals of Biochemistry - Life at the Molecular Level. 3rd ed. John Wiley & Sons, Inc. 2008</ref>. In addition to activating itself, it can also activate [http://www.proteopedia.org/wiki/index.php/Chymotrypsin chymotrypsin] and [http://www.proteopedia.org/wiki/index.php/Elastase elastase]. | |||
==References== | ==References== | ||
<references /> | <references /> | ||
