6a5i
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Pseudocerastes Persicus Trypsin Inhibitor== | |
| + | <StructureSection load='6a5i' size='340' side='right'caption='[[6a5i]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6a5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudocerastes_persicus Pseudocerastes persicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A5I FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=6a5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a5i OCA], [https://pdbe.org/6a5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a5i RCSB], [https://www.ebi.ac.uk/pdbsum/6a5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a5i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VKT_PSEPC VKT_PSEPC] Serine protease inhibitor that weakly inhibits trypsin (Ki=0.2 uM) (PubMed:30452896). May have potassium channel blocking activities (PubMed:30973886).<ref>PMID:30452896</ref> <ref>PMID:30973886</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The main purpose of this report is to investigate the structural property and new potential function of PPTI (Pseudocerastes Persicus Trypsin Inhibitor), a kunitz-type protein with inhibitory effect against trypsin proteolytic activity. Besides kunitz-type serine protease inhibitors, PPTI shows clear-cut similarities with dendrotoxins (DTXs), the other kunitz-type protein subfamily. The most important reason is the presence of functionally important residues of DTXs at correspondingly the same positions in PPTI. As such, we proposed the new ability of PPTI for inhibiting voltage-gated potassium channels and consequently its dual functionality. At first, we determined the solution structure of PPTI via Nuclear Magnetic Resonance (NMR) spectroscopy. Then by homology modeling, we constructed the model structure of trypsin-PPTI complex to confirm the same interaction pattern as trypsin-BPTI at complex interface. Finally, by Brownian dynamics (BD) simulations of PPTI NMR derived ensemble structure as ligand against homology model of human Kv1.1 potassium channel as receptor, we evaluated the potential DTX-like activity of PPTI. The results of our study support the proposed dual functionality of PPTI. | ||
| - | + | Structural characterization of PPTI, a kunitz-type protein from the venom of Pseudocerastes persicus.,Banijamali SE, Amininasab M, Zaeifi D PLoS One. 2019 Apr 11;14(4):e0214657. doi: 10.1371/journal.pone.0214657., eCollection 2019. PMID:30973886<ref>PMID:30973886</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6a5i" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudocerastes persicus]] | ||
| + | [[Category: Amininasab M]] | ||
Current revision
Pseudocerastes Persicus Trypsin Inhibitor
| |||||||||||
