3tc2: Difference between revisions
New page: '''Unreleased structure''' The entry 3tc2 is ON HOLD Authors: Meulenbroek, E.M., Thomassen, E.A.J., Pannu, N.S. Description: Crystal structure of potato serine protease inhibitor. |
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==Crystal structure of potato serine protease inhibitor.== | |||
<StructureSection load='3tc2' size='340' side='right'caption='[[3tc2]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tc2]] is a 3 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=3TC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TC2 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]] 1.6Å</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=3tc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tc2 OCA], [https://pdbe.org/3tc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tc2 RCSB], [https://www.ebi.ac.uk/pdbsum/3tc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tc2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric double-headed Kunitz-type serine protease inhibitor structure to be determined. PSPI has a beta-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified. | |||
Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato.,Meulenbroek EM, Thomassen EA, Pouvreau L, Abrahams JP, Gruppen H, Pannu NS Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):794-9. doi:, 10.1107/S090744491201222X. Epub 2012 Jun 15. PMID:22751664<ref>PMID:22751664</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3tc2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Solanum tuberosum]] | |||
[[Category: Meulenbroek EM]] | |||
[[Category: Pannu NS]] | |||
[[Category: Thomassen EAJ]] | |||
Latest revision as of 05:27, 21 November 2024
Crystal structure of potato serine protease inhibitor.Crystal structure of potato serine protease inhibitor.
Structural highlights
Publication Abstract from PubMedPotato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric double-headed Kunitz-type serine protease inhibitor structure to be determined. PSPI has a beta-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified. Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serine protease inhibitor from potato.,Meulenbroek EM, Thomassen EA, Pouvreau L, Abrahams JP, Gruppen H, Pannu NS Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):794-9. doi:, 10.1107/S090744491201222X. Epub 2012 Jun 15. PMID:22751664[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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