6ku8: Difference between revisions
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<StructureSection load='6ku8' size='340' side='right'caption='[[6ku8]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='6ku8' size='340' side='right'caption='[[6ku8]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ku8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6ku8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinovirus_C Rhinovirus C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KU8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG7:4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC+ACID+ETHYL+ESTER'>AG7</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG7:4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC+ACID+ETHYL+ESTER'>AG7</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=6ku8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ku8 OCA], [https://pdbe.org/6ku8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ku8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ku8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ku8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E5D8F2_9ENTO E5D8F2_9ENTO] | |||
<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 6ku8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6ku8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Human rhinovirus|Human rhinovirus]] | |||
*[[Virus protease 3D structures|Virus protease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rhinovirus C]] | ||
[[Category: | [[Category: Yuan S]] | ||
[[Category: | [[Category: Zhu L]] | ||
Latest revision as of 13:44, 22 November 2023
structure of HRV-C 3C protein with rupintrivirstructure of HRV-C 3C protein with rupintrivir
Structural highlights
FunctionPublication Abstract from PubMedHuman rhinoviruses (HRVs) are the predominant infectious agents for the common cold worldwide. The HRV-C species cause severe illnesses in children and are closely related to acute exacerbations of asthma. 3C protease, a highly conserved enzyme, cleaves the viral polyprotein during replication and assists the virus in escaping the host immune system. These key roles make 3C protease an important drug target. A few structures of 3Cs complexed with an irreversible inhibitor rupintrivir have been determined. These structures shed light on the determinants of drug specificity. Here we describe the structures of HRV-C15 3C in free and inhibitor-bound forms. The volume-decreased S1' subsite and half-closed S2 subsite, which were thought to be unique features of enterovirus A 3C proteases, appear in the HRV-C 3C protease. Rupintrivir assumes an "intermediate" conformation in the complex, which might open up additional avenues for the design of potent antiviral inhibitors. Analysis of the features of the three-dimensional structures and the amino acid sequences of 3C proteases suggest new applications for existing drugs. Structure of the HRV-C 3C-Rupintrivir Complex Provides New Insights for Inhibitor Design.,Yuan S, Fan K, Chen Z, Sun Y, Hou H, Zhu L Virol Sin. 2020 Feb 26. pii: 10.1007/s12250-020-00196-4. doi:, 10.1007/s12250-020-00196-4. PMID:32103448[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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