2k1q: Difference between revisions
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==NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor== | ==NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor== | ||
<StructureSection load='2k1q' size='340' side='right' caption='[[2k1q | <StructureSection load='2k1q' size='340' side='right'caption='[[2k1q]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k1q]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2k1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepacivirus_C Hepacivirus C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K1Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE3:4-(2-AMINOETHYL)-3-CHLOROBENZOIC+ACID'>FE3</scene>, <scene name='pdbligand=IBU:2-METHYLPROPYL+HYDROGEN+CARBONATE'>IBU</scene>, <scene name='pdbligand=OBF:(2S)-2-AMINO-4,4-DIFLUOROBUTANOIC+ACID'>OBF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2k1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k1q OCA], [https://pdbe.org/2k1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k1q RCSB], [https://www.ebi.ac.uk/pdbsum/2k1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k1q ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/P90191_9HEPC P90191_9HEPC] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2k1q" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus protease 3D structures|Virus protease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Hepacivirus C]] | ||
[[Category: Bazzo | [[Category: Large Structures]] | ||
[[Category: Cicero | [[Category: Bazzo R]] | ||
[[Category: Eliseo | [[Category: Cicero DO]] | ||
[[Category: Gallo | [[Category: Eliseo T]] | ||
[[Category: Pennestri | [[Category: Gallo M]] | ||
[[Category: Pennestri M]] | |||
Latest revision as of 11:32, 15 November 2023
NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitorNMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor
Structural highlights
FunctionPublication Abstract from PubMedWe present the first structure of a noncovalent inhibitor bound to the protease domain of hepatitis C virus NS3 protein (NS3p), solved by NMR. The inhibitor exploits interactions with the S' region of NS3p to form a long-lived complex, although the absence of negative charges strongly reduces the association rate. The inhibitor stabilizes the N-terminal domain of NS3p and the substrate-binding site, and correctly aligns catalytic His-Asp residues. These actions were previously attributed exclusively to the cofactor NS4A, which interacts with the N-terminal domain of the NS3p and functions as an activator in vivo. The structure of the inhibitor/NS3p complex is very similar to that of the NS3p-NS4A complex, showing that binding of the NS4A cofactor is not the only event leading to a stable active-site conformation. Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.,Gallo M, Pennestri M, Bottomley MJ, Barbato G, Eliseo T, Paci M, Narjes F, De Francesco R, Summa V, Koch U, Bazzo R, Cicero DO J Mol Biol. 2009 Jan 30;385(4):1142-55. Epub 2008 Nov 24. PMID:19061898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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