5fnx: Difference between revisions
New page: '''Unreleased structure''' The entry 5fnx is ON HOLD Authors: Guerra, Y., Rudino-Pinera, E. Description: Crystal structural at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of ... |
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The | ==Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0== | ||
<StructureSection load='5fnx' size='340' side='right'caption='[[5fnx]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fnx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FNX 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]] 2.65Å</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=5fnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fnx OCA], [https://pdbe.org/5fnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fnx RCSB], [https://www.ebi.ac.uk/pdbsum/5fnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fnx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M1AKE5_SOLTU M1AKE5_SOLTU] | |||
<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> | ||
[[Category: | <div class="pdbe-citations 5fnx" style="background-color:#fffaf0;"></div> | ||
[[Category: Guerra | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Solanum tuberosum]] | |||
[[Category: Guerra Y]] | |||
[[Category: Rudino-Pinera E]] | |||
Latest revision as of 10:00, 19 July 2023
Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0Crystal structure at pH 9.0 of a potato STI-Kunitz bi-functional inhibitor of serine and aspartic proteases in space group p4322 and ph 9.0
Structural highlights
FunctionPublication Abstract from PubMedBi-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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