1dp5: Difference between revisions

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[[Image:1dp5.~~gif~~|left|200px]]

[[Image:1dp5.png|left|200px]]

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~~'''~~THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR~~'''~~

===THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR===

~~==Overview==~~

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~~Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although~~ this ~~inhibitor consists of 68 residues~~, ~~we show that~~ the ~~inhibitory activity resides within~~ the ~~N-terminal half of the molecule. Structures solved~~ at 2.~~2 and 1~~.~~8 A~~, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the ~~free inhibitor has detectable intrinsic secondary structure in solution~~. ~~However, upon contact with the enzyme, residues 2~~-~~32 become ordered and adopt a near~~-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.

The line below this paragraph, {{ABSTRACT_PUBMED_10655612}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10655612 is the PubMed ID number.

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==About this Structure==

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[[Category: Mmm]]

[[Category: Proteinase some]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 14~~:06:19 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:21 2008''

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-[[Image:1dp5.gif|left|200px]]
+{{Seed}}
+[[Image:1dp5.png|left|200px]]
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 {{STRUCTURE_1dp5|  PDB=1dp5  |  SCENE=  }}
-'''THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR'''
+===THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR===
-==Overview==
+<!--
-Aspartic proteinase A from yeast is specifically and potently inhibited by a small protein called IA3 from Saccharomyces cerevisiae. Although this inhibitor consists of 68 residues, we show that the inhibitory activity resides within the N-terminal half of the molecule. Structures solved at 2.2 and 1.8 A, respectively, for complexes of proteinase A with full-length IA3 and with a truncated form consisting only of residues 2-34, reveal an unprecedented mode of inhibitor-enzyme interactions. Neither form of the free inhibitor has detectable intrinsic secondary structure in solution. However, upon contact with the enzyme, residues 2-32 become ordered and adopt a near-perfect alpha-helical conformation. Thus, the proteinase acts as a folding template, stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_10655612}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10655612 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10655612}}
 ==About this Structure==
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 [[Category: Mmm]]
 [[Category: Proteinase some]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:06:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:21 2008''