1f32

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:09, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1f32' size='340' side='right'caption='[[1f32]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1f32' size='340' side='right'caption='[[1f32]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1f32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascsu Ascsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F32 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1f32]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F32 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f34|1f34]]</div></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]] 1.75&#8491;</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=1f32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f32 OCA], [https://pdbe.org/1f32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f32 RCSB], [https://www.ebi.ac.uk/pdbsum/1f32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f32 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=1f32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f32 OCA], [https://pdbe.org/1f32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f32 RCSB], [https://www.ebi.ac.uk/pdbsum/1f32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/API3_ASCSU API3_ASCSU]] This is an inhibitor of the aspartic protease pepsin.
+
[https://www.uniprot.org/uniprot/API3_ASCSU API3_ASCSU] This is an inhibitor of the aspartic protease pepsin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1f32 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=1f32 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 1f32" style="background-color:#fffaf0;"></div>
 
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ascsu]]
+
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[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 inhibitor]]
+
-
[[Category: Proteinase inhibitor]]
+

Current revision

CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3

PDB ID 1f32

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools