4gch

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[[Image:4gch.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_4gch| PDB=4gch | SCENE= }}
{{STRUCTURE_4gch| PDB=4gch | SCENE= }}
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'''STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN'''
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===STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 2364065 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2364065}}
==About this Structure==
==About this Structure==
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[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:38:22 2008''

Revision as of 10:38, 3 July 2008

Image:4gch.png

Template:STRUCTURE 4gch

STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN

Template:ABSTRACT PUBMED 2364065

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

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