1fuj

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<StructureSection load='1fuj' size='340' side='right'caption='[[1fuj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1fuj' size='340' side='right'caption='[[1fuj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1fuj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1fuj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1fuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuj OCA], [https://pdbe.org/1fuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuj RCSB], [https://www.ebi.ac.uk/pdbsum/1fuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuj 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=1fuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuj OCA], [https://pdbe.org/1fuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuj RCSB], [https://www.ebi.ac.uk/pdbsum/1fuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PRTN3_HUMAN PRTN3_HUMAN]] Polymorphonuclear leukocyte serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema when administered by tracheal insufflation to hamsters.
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[https://www.uniprot.org/uniprot/PRTN3_HUMAN PRTN3_HUMAN] Polymorphonuclear leukocyte serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema when administered by tracheal insufflation to hamsters.
== 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=1fuj 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=1fuj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of PR3, a serine proteinase from the azurophilic granules of human polymorphonuclear neutrophils, has been solved by molecular replacement using the human leukocyte elastase structure. The PR3 structure has been refined to an R-factor (= sigma parallel Fo magnitude of-Fc parallel/sigma magnitude of Fo) of 0.201 for all data in the range of 10.0 to 2.2 A resolution. The enzyme was crystallized in space group P21 with four molecules in the asymmetric unit (Vm approximately equal to 2.6 A/Da). The overall fold consists of two domains of beta-barrel structures typical of the chymotrypsin family of serine proteinases. In general, the substrate binding sites, S4 to S3', are more polar than comparable sites in the related proteinase, human leukocyte elastase. The experimentally observed preference of PR3 for small aliphatic residues at the P1 position of a substrate is explained by the Val to Ile substitution at position 190 when compared to the elastase structure. The substitution of Ala by Asp at position 213 at the back of S1 should not affect its specificity greatly, as the Asp side-chain points back into the interior of the protein. The PR3 structure includes a disaccharide unit (N-linked 2-acetamido-2-deoxy-beta-D-glucopyranose and 1,6-linked alpha-L-fucopyranose) covalently attached to Asn 159. The linear antigenic sites of PR3 reported to react with Wegener's granulomatosis autoantibodies occur in regions of the three-dimensional structure that may implicate the inactive pro-form of the enzyme in the pathogenesis of the disease.
 
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The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies.,Fujinaga M, Chernaia MM, Halenbeck R, Koths K, James MN J Mol Biol. 1996 Aug 16;261(2):267-78. PMID:8757293<ref>PMID:8757293</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1fuj" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chernaia, M M]]
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[[Category: Chernaia MM]]
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[[Category: Fujinaga, M]]
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[[Category: Fujinaga M]]
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[[Category: Halenbeck, R]]
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[[Category: Halenbeck R]]
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[[Category: James, M N.G]]
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[[Category: James MNG]]
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[[Category: Koths, K]]
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[[Category: Koths K]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Serine protease]]
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[[Category: Zymogen]]
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Revision as of 11:16, 27 March 2024

PR3 (MYELOBLASTIN)

PDB ID 1fuj

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