6yd3
From Proteopedia
(Difference between revisions)
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==X-ray structure of furin in complex with the canavanine derived inhibitor 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Arg-Amba== | ==X-ray structure of furin in complex with the canavanine derived inhibitor 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Arg-Amba== | ||
| - | <StructureSection load='6yd3' size='340' side='right'caption='[[6yd3]]' scene=''> | + | <StructureSection load='6yd3' size='340' side='right'caption='[[6yd3]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YD3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yd3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YD3 FirstGlance]. <br> |
| - | </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=6yd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yd3 OCA], [https://pdbe.org/6yd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yd3 RCSB], [https://www.ebi.ac.uk/pdbsum/6yd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yd3 ProSAT]</span></td></tr> | + | </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=2UE:1-[4-(2-OXOETHYL)BENZYL]GUANIDINE'>2UE</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=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ON8:1-[(3~{S})-3-azanyl-4-oxidanylidene-butoxy]guanidine'>ON8</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TBG:3-METHYL-L-VALINE'>TBG</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FURIN, FUR, PACE, PCSK3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Furin Furin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.75 3.4.21.75] </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=6yd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yd3 OCA], [https://pdbe.org/6yd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yd3 RCSB], [https://www.ebi.ac.uk/pdbsum/6yd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yd3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Furin 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<ref>PMID:33732412</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yd3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Furin]] | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dahms | + | [[Category: Dahms, S O]] |
| + | [[Category: Canavanine]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Protease]] | ||
Revision as of 10:44, 31 March 2021
X-ray structure of furin in complex with the canavanine derived inhibitor 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Arg-Amba
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Categories: Furin | Human | Large Structures | Dahms, S O | Canavanine | Complex | Hydrolase | Inhibitor | Protease
