5fzy: Difference between revisions
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==CRYSTAL STRUCTURE OF N19D POTATO STI-KUNITZ BI-FUNCTIONAL INHIBITOR OF SERINE AND ASPARTIC PROTEASES IN SPACE GROUP C2221 AND PH 3.5== | |||
<StructureSection load='5fzy' size='340' side='right' caption='[[5fzy]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fzy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FZY FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fzu|5fzu]], [[5fzz|5fzz]], [[5g00|5g00]]</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=5fzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzy OCA], [http://pdbe.org/5fzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzy RCSB], [http://www.ebi.ac.uk/pdbsum/5fzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzy ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylated proteins able to inhibit serine and aspartic proteases. Here we report six crystal structures of the wild-type and a non-glycosylated mutant of the bifunctional inhibitor E3Ad obtained at different pH values and space groups. The crystal structures show that E3Ad adopts the typical beta-trefoil fold of the STI family exhibiting some conformational changes due to pH variations and crystal packing. Despite the high sequence identity with a recently reported potato cathepsin D inhibitor (PDI), three-dimensional structures obtained in this work show a significant conformational change in the protease-binding loop proposed for aspartic protease inhibition. The E3Ad binding loop for serine protease inhibition is also proposed, based on structural similarity with a novel non-canonical conformation described for the double-headed inhibitor API-A from the Kunitz-type STI family. In addition, structural and sequence analyses suggest that bifunctional inhibitors of serine and aspartic proteases from the Kunitz-type STI family are more similar to double-headed inhibitor API-A than other inhibitors with a canonical protease-binding loop. | |||
Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?,Guerra Y, Valiente PA, Pons T, Berry C, Rudino-Pinera E J Struct Biol. 2016 Aug;195(2):259-71. doi: 10.1016/j.jsb.2016.06.014. Epub 2016 , Jun 18. PMID:27329566<ref>PMID:27329566</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fzy" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Guerra, Y]] | |||
[[Category: Rudino-Pinera, E]] | [[Category: Rudino-Pinera, E]] | ||
[[Category: | [[Category: Aspartic protease]] | ||
[[Category: Bi-functional protease inhibitor]] | |||
[[Category: Hydrolase]] | |||
[[Category: Hydrolase inhibitor]] | |||
[[Category: Kunitz-type inhibitor]] | |||
[[Category: Protease inhibitor]] | |||
[[Category: Serine protease]] | |||
[[Category: Sti-kunitz inhibitor]] | |||
