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Sandbox wabash15
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proteopedia linkproteopedia link "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.
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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 (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
Trypsin in a globular protein that is in the Serine protease family. Trypsin uses the 'catalytic triad'
Disease
Relevance
Structural highlights
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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