Lotem haleva/test page

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==Your Heading Here (maybe something like 'Structure')==
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==Trypsin==
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<StructureSection load='1y3v' size='340' side='right' caption='Trysine' scene=''>
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<StructureSection load='1y3v' size='340' side='right' caption='Bovine trypsine complex with inhibitor and Ca+2 ion (green) (PDB code [[1y3v]])' scene=''>
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This is a default text for your page '''Lotem haleva/test page'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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'''Trypsin''' is a serine protease that found in the digestive system of many vertebrates, where it hydrolyses proteins<ref>doi:10.1016/0076-6879(94)44004-2</ref>.
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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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Trypsin is produced in the pancreas as the inactive zymogen protease called trypsinogen. trypsinogen secreted into the small intestine where it activates trypsinogen into trypsin by the enzyme Antrookinaz using proteolytic decomposition.
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Trypsin Break peptide chains at the carboxyl side of the amino acids lysine or arginine,
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is a serine protease, found in the digestive system of many vertebrates, where it hydrolyses proteins<ref>doi:10.1016/0076-6879(94)44004-2</ref>.
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except when it is followed by proline. .
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Trypsin is produced in the pancreas as the inactive protease trypsinogen.
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Trypsin Break peptide chains mainly at the carboxyl side of the amino acids lysine or arginine,
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except when either is followed by proline. It is used for numerous biotechnological processes.
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The process is commonly referred to as trypsin proteolysis or trypsinisation,
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and proteins that have been digested/treated with trypsin are said to have been trypsinized.
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== Function ==
== Function ==
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In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides.
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Trypsin catalyzes the hydrolysis of peptide bonds and cutting proteins into smaller peptides in the duodenum.
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The enzymatic mechanism is similar to that of other serine proteases. These enzymes contain a catalytic triad consisting of <scene name='60/607865/Active_site/2'>histidine-57, aspartate-102, and serine-195</scene>. These three residues form a charge relay that serves to make the active site serine nucleophilic
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== Structure and Mechanism ==
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== Disease ==
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Trypsin is a medium size globular protein that contains either <scene name='60/607865/Helix/1'>alpha helix</scene> and <scene name='60/607865/Sheets/1'>beta sheets</scene>.
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The enzymatic mechanism of Trypsin is similar to the other serine proteases. These enzymes contain a catalytic triad consisting of <scene name='60/607865/Active_site/2'>histidine-57, aspartate-102, and serine-195</scene>, These three residues makes the active site serine nucleophilic <ref>doi:10.1007/s00018-005-5160-x</ref>.
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Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.
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The <scene name='60/607865/Asp_189/1'>aspartate residue</scene> located in the catalytic pocket of trypsin is responsible for attracting and stabilizing positively charged lysine or arginine, and as a result responsible for the specificity of the enzyme <ref> doi:10.1021/pr0705035</ref>.
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== Relevance ==
 
== Structural highlights ==
== Structural highlights ==
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There are different ways to present the protein structure :<scene name='60/607865/Balls_and_stik/1'>balls and stick</scene>, <scene name='60/607865/Surface/1'>surface</scene> and <scene name='60/607865/Backbone/1'>Backbone</scene>. Another way to view the protein is <scene name='60/607865/Rainbow_n_to_c/1'>Rainbow</scene> that show the protein from the N (blue) to C terminal (green).
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

Trypsin

Bovine trypsine complex with inhibitor and Ca+2 ion (green) (PDB code 1y3v)

Drag the structure with the mouse to rotate

References

  1. ↑ Rawlings ND, Barrett AJ. Families of serine peptidases. Methods Enzymol. 1994;244:19-61. doi: 10.1016/0076-6879(94)44004-2. PMID:7845208 doi:http://dx.doi.org/10.1016/0076-6879(94)44004-2
  2. ↑ Polgar L. The catalytic triad of serine peptidases. Cell Mol Life Sci. 2005 Oct;62(19-20):2161-72. PMID:16003488 doi:http://dx.doi.org/10.1007/s00018-005-5160-x
  3. ↑ Rodriguez J, Gupta N, Smith RD, Pevzner PA. Does trypsin cut before proline? J Proteome Res. 2008 Jan;7(1):300-5. Epub 2007 Dec 8. PMID:18067249 doi:http://dx.doi.org/10.1021/pr0705035

Proteopedia Page Contributors and Editors (what is this?)

Lotem Haleva, Michal Harel

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