1f34: Difference between revisions

Revision as of 13:34, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1F34 is a Protein complex structure of sequences from Ascaris suum and Sus scrofa with as ligand. Active as Pepsin A, with EC number 3.4.23.1 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:34:16 2008

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OCA

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-[[Image:1f34.gif|left|200px]]<br /><applet load="1f34" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f34.gif|left|200px]]<br /><applet load="1f34" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f34, resolution 2.45&Aring;" />
 '''CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN'''<br />
 ==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 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==
-F34 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA].
+F34 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Protein complex]]
 [[Category: Sus scrofa]]
-[[Category: Cherney, M.M.]]
+[[Category: Cherney, M M.]]
 [[Category: Garen, C.]]
-[[Category: James, M.N.]]
+[[Category: James, M N.]]
-[[Category: Ng, K.K.]]
+[[Category: Ng, K K.]]
-[[Category: Petersen, J.F.]]
+[[Category: Petersen, J F.]]
 [[Category: MPD]]
 [[Category: proteinase-inhibitor complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:34:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:16 2008''