1f34: Difference between revisions

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<StructureSection load='1f34' size='340' side='right'caption='[[1f34]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='1f34' size='340' side='right'caption='[[1f34]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascsu Ascsu] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F34 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F34 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f32|1f32]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f34 OCA], [https://pdbe.org/1f34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f34 RCSB], [https://www.ebi.ac.uk/pdbsum/1f34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f34 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f34 OCA], [https://pdbe.org/1f34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f34 RCSB], [https://www.ebi.ac.uk/pdbsum/1f34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f34 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG]] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. [[https://www.uniprot.org/uniprot/API3_ASCSU API3_ASCSU]] This is an inhibitor of the aspartic protease pepsin.  
[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f34 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f34 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:10932249</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1f34" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Pepsin|Pepsin]]
*[[Pepsin|Pepsin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ascsu]]
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pepsin A]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Cherney, M M]]
[[Category: Cherney MM]]
[[Category: Garen, C]]
[[Category: Garen C]]
[[Category: James, M N]]
[[Category: James MN]]
[[Category: Ng, K K]]
[[Category: Ng KK]]
[[Category: Petersen, J F]]
[[Category: Petersen JF]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Proteinase-inhibitor complex]]

Latest revision as of 13:09, 20 March 2024

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

Structural highlights

1f34 is a 2 chain structure with sequence from Ascaris suum and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PEPA_PIG Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f34, resolution 2.45Å

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