4q80: Difference between revisions

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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]] 3.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4q80]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q80 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q7x|4q7x]], [[4q7y|4q7y]], [[4q7z|4q7z]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q80 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q80 RCSB], [http://www.ebi.ac.uk/pdbsum/4q80 PDBsum]</span></td></tr>
<table>
<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.


The entry 4q80 is ON HOLD  until Paper Publication
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>


Authors: Eigenbrot, C., Lin, S.J., Dong, K.C.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Neutrophil serine protease 4 (PRSS57) with val-leu-lys-chloromethylketone (VLK-cmk)
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dong, K C.]]
[[Category: Eigenbrot, C.]]
[[Category: Lin, S J.]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Peptidase]]
[[Category: Trypsin homology]]
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