1f32
From Proteopedia
(New page: 200px<br /><applet load="1f32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f32, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1f32.gif|left|200px]]<br /><applet load="1f32" size=" | + | [[Image:1f32.gif|left|200px]]<br /><applet load="1f32" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f32, resolution 1.75Å" /> | caption="1f32, resolution 1.75Å" /> | ||
'''CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3'''<br /> | '''CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1F32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http:// | + | 1F32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F32 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ascaris suum]] | [[Category: Ascaris suum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cherney, M | + | [[Category: Cherney, M M.]] |
[[Category: Garen, C.]] | [[Category: Garen, C.]] | ||
| - | [[Category: James, M | + | [[Category: James, M N.]] |
| - | [[Category: Ng, K | + | [[Category: Ng, K K.]] |
| - | [[Category: Petersen, J | + | [[Category: Petersen, J F.]] |
[[Category: proteinase inhibitor]] | [[Category: proteinase inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:16 2008'' |
Revision as of 10:34, 21 February 2008
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CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3
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.
About this Structure
1F32 is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.
Reference
Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3., Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN, Nat Struct Biol. 2000 Aug;7(8):653-7. PMID:10932249
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