4gch

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[[Image:4gch.jpg|left|200px]]
[[Image:4gch.jpg|left|200px]]
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{{Structure
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|PDB= 4gch |SIZE=350|CAPTION= <scene name='initialview01'>4gch</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_4gch", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DMC:3-(4-DIETHYLAMINO-2-HYDROXY-PHENYL)-2-METHYL-PROPIONIC+ACID'>DMC</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_4gch| PDB=4gch | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gch OCA], [http://www.ebi.ac.uk/pdbsum/4gch PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4gch RCSB]</span>
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}}
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'''STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN'''
'''STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN'''
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[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:51 2008''
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Revision as of 19:24, 4 May 2008

Image:4gch.jpg

Template:STRUCTURE 4gch

STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN


Overview

The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.

About this Structure

4GCH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:2364065 Page seeded by OCA on Sun May 4 22:24:25 2008

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