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4q80
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Neutrophil serine protease 4 (PRSS57) with val-leu-lys-chloromethylketone (VLK-cmk)== | |
| + | <StructureSection load='4q80' size='340' side='right'caption='[[4q80]], [[Resolution|resolution]] 3.07Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q80]] is a 2 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=4Q80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q80 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.07Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2YS:D-VALYL-N-[(2S,3S)-7-AMINO-1-CHLORO-2-HYDROXYHEPTAN-3-YL]-L-LEUCINAMIDE'>2YS</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=4q80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q80 OCA], [https://pdbe.org/4q80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q80 RCSB], [https://www.ebi.ac.uk/pdbsum/4q80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q80 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRS57_HUMAN PRS57_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Trypsin-fold proteases, the largest mammalian protease family, are classified by their primary substrate specificity into one of three categories, trypsin-like, chymotrypsin-like, and elastase-like, based on key structural features of their active site. However, the recently discovered neutrophil serine protease 4 (NSP4, also known as PRSS57) presents a paradox: NSP4 exhibits a trypsin-like specificity for cleaving substrates after arginine residues, but it bears elastase-like specificity determining residues in the active site. Here we show that NSP4 has a fully occluded S1 pocket and that the substrate P1-arginine adopts a noncanonical "up" conformation stabilized by a solvent-exposed H-bond network. This uncommon arrangement, conserved in all NSP4 orthologs, enables NSP4 to process substrates after both arginine as well as post-translationally modified arginine residues, such as methylarginine and citrulline. These findings establish a distinct paradigm for substrate recognition by a trypsin-fold protease and provide insights into the function of NSP4. | ||
| - | + | Structures of Neutrophil Serine Protease 4 Reveal an Unusual Mechanism of Substrate Recognition by a Trypsin-Fold Protease.,Lin SJ, Dong KC, Eigenbrot C, van Lookeren Campagne M, Kirchhofer D Structure. 2014 Aug 19. pii: S0969-2126(14)00238-X. doi:, 10.1016/j.str.2014.07.008. PMID:25156428<ref>PMID:25156428</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4q80" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dong KC]] | ||
| + | [[Category: Eigenbrot C]] | ||
| + | [[Category: Lin SJ]] | ||
Current revision
Neutrophil serine protease 4 (PRSS57) with val-leu-lys-chloromethylketone (VLK-cmk)
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