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==X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba== | ==X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba== | ||
<StructureSection load='4omc' size='340' side='right' caption='[[4omc]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4omc' size='340' side='right'caption='[[4omc]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4omc]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4omc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=2UC:1-[3-(2-OXOETHYL)BENZYL]GUANIDINE'>2UC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_001220:meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine'>PRD_001220</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=4omc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omc OCA], [https://pdbe.org/4omc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omc RCSB], [https://www.ebi.ac.uk/pdbsum/4omc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | [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> | ||
<table> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 16: | ||
X-ray Structures of Human Furin in Complex with Competitive Inhibitors.,Dahms SO, Hardes K, Becker GL, Steinmetzer T, Brandstetter H, Than ME ACS Chem Biol. 2014 Apr 1. PMID:24666235<ref>PMID:24666235</ref> | X-ray Structures of Human Furin in Complex with Competitive Inhibitors.,Dahms SO, Hardes K, Becker GL, Steinmetzer T, Brandstetter H, Than ME ACS Chem Biol. 2014 Apr 1. PMID:24666235<ref>PMID:24666235</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4omc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Furin|Furin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Dahms | [[Category: Dahms SO]] | ||
[[Category: Than | [[Category: Than ME]] | ||
Latest revision as of 10:16, 27 November 2024
X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-AmbaX-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba
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 inhibitors are promising therapeutics for the treatment of cancer and numerous infections caused by bacteria and viruses, including the highly lethal Bacillus anthracis or the pandemic influenza virus. Development and improvement of inhibitors for pharmacological use require a detailed knowledge of the protease's substrate and inhibitor binding properties. Here we present a novel preparation of human furin and the first crystal structures of this enzyme in complex with noncovalent inhibitors. We show the inhibitor exchange by soaking, allowing the investigation of additional inhibitors and substrate analogues. Thus, our work provides a basis for the rational design of furin inhibitors. X-ray Structures of Human Furin in Complex with Competitive Inhibitors.,Dahms SO, Hardes K, Becker GL, Steinmetzer T, Brandstetter H, Than ME ACS Chem Biol. 2014 Apr 1. PMID:24666235[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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