Sandbox wabash23
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='72/725332/Active_site/1'>active site</scene> involves the residues SER 195, HIS 57, Asp 102 and GLY 193 in which the trypsin substrate forms a stable tetrahedral intermediate upon the formation of H-bonds located in what is known as the "oxyanion hole". This preferential binding of the enzyme-substrate complex of the acyl-enzyme intermediate is responsible for much of the catalytic efficiency of serine proteases. | + | The main transition state of interest of interest is the <scene name='72/725332/Acyl-intermediate/1'>acyl-intermediate</scene>which forms when the peptide bond of the newly bound substrate complex (as a tetrahedral intermediate) is cleaved yielding a carbonyl group on SER 195. The <scene name='72/725332/Active_site/1'>active site</scene> involves the residues SER 195, HIS 57, Asp 102 and GLY 193 in which the trypsin substrate forms a stable tetrahedral intermediate upon the formation of H-bonds located in what is known as the "oxyanion hole" which is located between SER 195 and GLY 193. This preferential binding of the enzyme-substrate complex of the acyl-enzyme intermediate is responsible for much of the catalytic efficiency of serine proteases. |
| - | 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. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:39, 19 February 2016
The Mechanism of Trypsin
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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
- ↑ Radisky ES, Lee JM, Lu CJ, Koshland DE Jr. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
