View source for 6ku8


==structure of HRV-C 3C protein with rupintrivir==
<StructureSection load='6ku8' size='340' side='right'caption='[[6ku8]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ku8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_c Human 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 [http://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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ku8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ku8 OCA], [http://pdbe.org/6ku8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ku8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ku8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ku8 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human 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<ref>PMID:32103448</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ku8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human rhinovirus c]]
[[Category: Large Structures]]
[[Category: Yuan, S]]
[[Category: Zhu, L]]
[[Category: Hrv]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Rupintrivir]]