3rc6

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==Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease==
==Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease==
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<StructureSection load='3rc6' size='340' side='right' caption='[[3rc6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='3rc6' size='340' side='right'caption='[[3rc6]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus_subtype_1a Hepatitis c virus subtype 1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RC6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rc6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_C_virus_genotype_1a Hepatitis C virus genotype 1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RC6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rc4|3rc4]], [[3rc5|3rc5]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31646 Hepatitis C virus subtype 1a])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rc6 OCA], [https://pdbe.org/3rc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rc6 RCSB], [https://www.ebi.ac.uk/pdbsum/3rc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rc6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rc6 OCA], [http://pdbe.org/3rc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rc6 RCSB], [http://www.ebi.ac.uk/pdbsum/3rc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rc6 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A8DG50_9HEPC A8DG50_9HEPC]
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Hepatitis C NS3/4A protease is a prime therapeutic target responsible for cleaving the viral polyprotein at junctions 3-4A, 4A4B, 4B5A and 5A5B, and two host-cell adapter proteins of the innate immune response, TRIF and MAVS. In this study, NS3/4A crystal structures of both host-cell cleavage sites are determined and compared to the crystal structures of viral substrates. Two distinct protease conformations are observed and correlate with substrate specificity: (1) 3-4A, 4A4B, 5A5B and MAVS, which are processed more efficiently by the protease, form extensive electrostatic networks when in complex with the protease and (2) TRIF and 4B5A, which contain polyproline motifs in their full-length sequences, do not form electrostatic networks in their crystal complexes. These findings provide mechanistic insights into NS3/4A substrate recognition, which may assist in a more rational approach to inhibitor design in the face of the rapid acquisition of resistance.
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Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease.,Romano KP, Laine JM, Deveau LM, Cao H, Massi F, Schiffer CA J Virol. 2011 Apr 20. PMID:21507982<ref>PMID:21507982</ref>
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==See Also==
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*[[Virus protease 3D structures|Virus protease 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rc6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hepatitis c virus subtype 1a]]
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[[Category: Hepatitis C virus genotype 1a]]
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[[Category: Romano, K P]]
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[[Category: Large Structures]]
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[[Category: Schiffer, C A]]
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[[Category: Romano KP]]
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[[Category: Drug design]]
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[[Category: Schiffer CA]]
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[[Category: Drug resistance]]
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[[Category: Hydrolase]]
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[[Category: Protease inhibitor]]
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[[Category: Serine protease]]
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[[Category: Viral protein]]
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Current revision

Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease

PDB ID 3rc6

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