6ku7: Difference between revisions
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==structure of HRV-C 3C protein== | |||
<StructureSection load='6ku7' size='340' side='right'caption='[[6ku7]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ku7]] 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=6KU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KU7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=6ku7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ku7 OCA], [https://pdbe.org/6ku7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ku7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ku7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ku7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E5D8F2_9ENTO E5D8F2_9ENTO] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ku7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus protease 3D structures|Virus protease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhinovirus C]] | |||
[[Category: Yuan S]] | |||
[[Category: Zhu L]] | |||
