1lw6: Difference between revisions

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[[Image:1lw6.~~gif~~|left|200px]]

[[Image:1lw6.png|left|200px]]

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~~'''~~Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution~~'''~~

===Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution===

~~==Overview==~~

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~~A classical peptide inhibitor of serine proteases that is hydrolyzed approximately 10(7) times more slowly than a good substrate is shown to form an acyl-enzyme intermediate rapidly. Despite~~ this ~~quick first step~~, ~~further reaction is slowed dramatically because of tight and oriented binding of~~ the ~~cleaved peptide, preventing acyl-enzyme hydrolysis and favoring~~ the ~~reverse reaction~~. ~~Moreover~~, this mechanism appears to be common to a large class of tight-binding serine protease inhibitors that mimic good substrates. The arrest of enzymatic reaction at the intermediate stage allowed us to determine that the consensus nucleophilic attack angle is ~~close to 90 degrees in~~ the ~~reactive Michaelis complexes~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12142461}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12142461 is the PubMed ID number.

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==About this Structure==

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[[Category: Inhibitor]]

[[Category: Serine protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:21:31 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:36:52 2008''

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-[[Image:1lw6.gif|left|200px]]
+{{Seed}}
+[[Image:1lw6.png|left|200px]]
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 {{STRUCTURE_1lw6|  PDB=1lw6  |  SCENE=  }}
-'''Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution'''
+===Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution===
-==Overview==
+<!--
-A classical peptide inhibitor of serine proteases that is hydrolyzed approximately 10(7) times more slowly than a good substrate is shown to form an acyl-enzyme intermediate rapidly. Despite this quick first step, further reaction is slowed dramatically because of tight and oriented binding of the cleaved peptide, preventing acyl-enzyme hydrolysis and favoring the reverse reaction. Moreover, this mechanism appears to be common to a large class of tight-binding serine protease inhibitors that mimic good substrates. The arrest of enzymatic reaction at the intermediate stage allowed us to determine that the consensus nucleophilic attack angle is close to 90 degrees in the reactive Michaelis complexes.
+The line below this paragraph, {{ABSTRACT_PUBMED_12142461}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12142461 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12142461}}
 ==About this Structure==
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 [[Category: Inhibitor]]
 [[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:21:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:36:52 2008''