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| | ==Neutrophil serine protease 4 (PRSS57) apo form 1== | | ==Neutrophil serine protease 4 (PRSS57) apo form 1== |
| - | <StructureSection load='4q7x' size='340' side='right' caption='[[4q7x]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='4q7x' size='340' side='right'caption='[[4q7x]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q7x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q7X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q7x]] 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=4Q7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q7X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q7y|4q7y]], [[4q7z|4q7z]], [[4q80|4q80]]</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=4q7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7x OCA], [https://pdbe.org/4q7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q7x RCSB], [https://www.ebi.ac.uk/pdbsum/4q7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7x ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRSS57, PRSSL1, UNQ782/PRO1599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q7x OCA], [http://pdbe.org/4q7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q7x RCSB], [http://www.ebi.ac.uk/pdbsum/4q7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q7x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PRS57_HUMAN PRS57_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Dong, K C]] | + | [[Category: Large Structures]] |
| - | [[Category: Eigenbrot, C]] | + | [[Category: Dong KC]] |
| - | [[Category: Lin, S J]] | + | [[Category: Eigenbrot C]] |
| - | [[Category: Hydrolase]] | + | [[Category: Lin SJ]] |
| - | [[Category: Peptidase]]
| + | |
| - | [[Category: Trypsin homology]]
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| Structural highlights
Function
PRS57_HUMAN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lin SJ, Dong KC, Eigenbrot C, van Lookeren Campagne M, Kirchhofer D. Structures of Neutrophil Serine Protease 4 Reveal an Unusual Mechanism of Substrate Recognition by a Trypsin-Fold Protease. Structure. 2014 Aug 19. pii: S0969-2126(14)00238-X. doi:, 10.1016/j.str.2014.07.008. PMID:25156428 doi:http://dx.doi.org/10.1016/j.str.2014.07.008
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