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5fzu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF N19D POTATO STI-KUNITZ BI-FUNCTIONAL INHIBITOR OF SERINE AND ASPARTIC PROTEASES IN SPACE GROUP P4322 AND PH 7.2== | |
| + | <StructureSection load='5fzu' size='340' side='right' caption='[[5fzu]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fzu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FZU FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fzy|5fzy]], [[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=5fzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fzu OCA], [http://pdbe.org/5fzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fzu RCSB], [http://www.ebi.ac.uk/pdbsum/5fzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fzu 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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5fzu" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Guerra, Y]] | [[Category: Guerra, Y]] | ||
| + | [[Category: Rudino-Pinero, E]] | ||
| + | [[Category: Bi-functional protease inhibitor]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase inhibitor]] | ||
| + | [[Category: Kunitz-type inhibitor]] | ||
| + | [[Category: Protease inhibitor]] | ||
| + | [[Category: Protease]] | ||
Revision as of 02:21, 13 July 2016
CRYSTAL STRUCTURE OF N19D POTATO STI-KUNITZ BI-FUNCTIONAL INHIBITOR OF SERINE AND ASPARTIC PROTEASES IN SPACE GROUP P4322 AND PH 7.2
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