6yd7: Difference between revisions
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<StructureSection load='6yd7' size='340' side='right'caption='[[6yd7]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6yd7' size='340' side='right'caption='[[6yd7]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6yd7]] is a | <table><tr><td colspan='2'>[[6yd7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YD7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=00S:4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE'>00S</scene>, <scene name='pdbligand=3U0:2-[4-(carbamimidamidomethyl)phenyl]ethanoic+acid'>3U0</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GGB:L-CANAVANINE'>GGB</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TBG:3-METHYL-L-VALINE'>TBG</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=6yd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yd7 OCA], [https://pdbe.org/6yd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yd7 RCSB], [https://www.ebi.ac.uk/pdbsum/6yd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yd7 ProSAT]</span></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=6yd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yd7 OCA], [https://pdbe.org/6yd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yd7 RCSB], [https://www.ebi.ac.uk/pdbsum/6yd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yd7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FURIN_HUMAN FURIN_HUMAN] Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.<ref>PMID:7690548</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6yd7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6yd7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Furin|Furin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Dahms SO]] | ||
Latest revision as of 13:53, 15 November 2023
Structural highlights
FunctionFURIN_HUMAN Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.[1] Publication Abstract from PubMedFurin activates numerous viral glycoproteins, and its inhibition prevents virus replication and spread. Through the replacement of arginine by the less basic canavanine, new inhibitors targeting furin in the trans-Golgi network were developed. These inhibitors exert potent antiviral activity in cell culture with much lower toxicity than arginine-derived analogues, most likely due to their reduced protonation in the blood circulation. Thus, despite its important physiological functions, furin might be a suitable antiviral drug target. The Basicity Makes the Difference: Improved Canavanine-Derived Inhibitors of the Proprotein Convertase Furin.,Lam van TV, Heindl MR, Schlutt C, Bottcher-Friebertshauser E, Bartenschlager R, Klebe G, Brandstetter H, Dahms SO, Steinmetzer T ACS Med Chem Lett. 2021 Feb 9;12(3):426-432. doi: 10.1021/acsmedchemlett.0c00651., eCollection 2021 Mar 11. PMID:33732412[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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