6mrq: Difference between revisions
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==Structure of ToPI1 inhibitor from Tityus obscurus scorpion venom in complex with trypsin== | |||
<StructureSection load='6mrq' size='340' side='right'caption='[[6mrq]], [[Resolution|resolution]] 1.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mrq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Tityus Tityus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MRQ 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]] 1.288Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6mrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mrq OCA], [https://pdbe.org/6mrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mrq RCSB], [https://www.ebi.ac.uk/pdbsum/6mrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mrq ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptidase inhibitors (PIs) have been broadly studied due to their wide therapeutic potential for human diseases. A potent trypsin inhibitor from Tityus obscurus scorpion venom was characterized and named ToPI1, with 33 amino acid residues and three disulfide bonds. The X-ray structure of the ToPI1:trypsin complex, in association with the mass spectrometry data, indicate a sequential set of events: the complex formation with the inhibitor Lys(32) in the trypsin S1 pocket, the inhibitor C-terminal residue Ser(33) cleavage, and the cyclization of ToPI1 via a peptide bond between residues Ile(1) and Lys(32). Kinetic and thermodynamic characterization of the complex was obtained. ToPI1 shares no sequence similarity with other PIs characterized to date and is the first PI with CS-alpha/beta motif described from animal venoms. In its cyclic form, it shares structural similarities with plant cyclotides that also inhibit trypsin. These results bring new insights for studies with venom compounds, PIs, and drug design. | |||
Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides.,Mourao CBF, Brand GD, Fernandes JPC, Prates MV, Bloch C Jr, Barbosa JARG, Freitas SM, Restano-Cassulini R, Possani LD, Schwartz EF J Med Chem. 2020 Aug 12. doi: 10.1021/acs.jmedchem.0c00686. PMID:32787139<ref>PMID:32787139</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6mrq" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin 3D structures|Trypsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Tityus]] | |||
[[Category: Barbosa JARG]] | |||
[[Category: Fernandes JC]] | |||
[[Category: Mourao CBF]] | |||
[[Category: Schwartz EF]] | |||