1f34: Difference between revisions

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[[Image:1f34.~~gif~~|left|200px]]

[[Image:1f34.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN~~'''~~

===CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN===

~~==Overview==~~

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The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and 2.45 A resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this ~~unique inhibitor. PI-3 has a new fold consisting of two domains~~, ~~each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex~~, the ~~N-terminal beta-strand of PI-3 pairs with one strand of~~ the ~~'active site flap'~~ (~~residues 70-82~~) ~~of pepsin~~, ~~thus forming an eight-stranded beta-sheet that spans~~ the ~~two proteins~~. PI-~~3 has a novel mode of inhibition, using its N~~-terminal residues to occupy and therefore block the first three binding pockets in pepsin for substrate residues C-terminal to the scissile bond (S1'-S3'). The molecular structure of the pepsin-PI-3 complex suggests new avenues for the rational design of proteinaceous aspartic proteinase inhibitors.

The line below this paragraph, {{ABSTRACT_PUBMED_10932249}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10932249 is the PubMed ID number.

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==About this Structure==

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[[Category: Petersen, J F.]]

[[Category: Proteinase-inhibitor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:50:07 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:34:02 2008''

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-[[Image:1f34.gif|left|200px]]
+{{Seed}}
+[[Image:1f34.png|left|200px]]
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 {{STRUCTURE_1f34|  PDB=1f34  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN'''
+===CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN===
-==Overview==
+<!--
-The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and 2.45 A resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this unique inhibitor. PI-3 has a new fold consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the 'active site flap' (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that spans the two proteins. PI-3 has a novel mode of inhibition, using its N-terminal residues to occupy and therefore block the first three binding pockets in pepsin for substrate residues C-terminal to the scissile bond (S1'-S3'). The molecular structure of the pepsin-PI-3 complex suggests new avenues for the rational design of proteinaceous aspartic proteinase inhibitors.
+The line below this paragraph, {{ABSTRACT_PUBMED_10932249}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10932249 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10932249}}
 ==About this Structure==
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 [[Category: Petersen, J F.]]
 [[Category: Proteinase-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:50:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:34:02 2008''