3d23

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[[Image:3d23.png|left|200px]]
 
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{{STRUCTURE_3d23| PDB=3d23 | SCENE= }}
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==Main protease of HCoV-HKU1==
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<StructureSection load='3d23' size='340' side='right'caption='[[3d23]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3d23]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_HKU1_(isolate_N1) Human coronavirus HKU1 (isolate N1)] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D23 FirstGlance]. <br>
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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]] 2.5&#8491;</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=010:PHENYLMETHANOL'>010</scene>, <scene name='pdbligand=02J:5-METHYL-1,2-OXAZOLE-3-CARBOXYLIC+ACID'>02J</scene>, <scene name='pdbligand=PJE:(E,4S)-4-AZANYL-5-[(3S)-2-OXIDANYLIDENEPYRROLIDIN-3-YL]PENT-2-ENOIC+ACID'>PJE</scene></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=3d23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d23 OCA], [https://pdbe.org/3d23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d23 RCSB], [https://www.ebi.ac.uk/pdbsum/3d23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d23 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/R1A_CVHN1 R1A_CVHN1] The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).[PROSITE-ProRule:PRU00772] Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures.[UniProtKB:P0DTC1] Binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/3d23_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d23 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The newly emergent human coronavirus HKU1 (HCoV-HKU1) was first identified in Hong Kong in 2005. Infection by HCoV-HKU1 occurs worldwide and causes syndromes such as the common cold, bronchitis, and pneumonia. The CoV main protease (M(pro)), which is a key enzyme in viral replication via the proteolytic processing of the replicase polyproteins, has been recognized as an attractive target for rational drug design. In this study, we report the structure of HCoV-HKU1 M(pro) in complex with a Michael acceptor, inhibitor N3. The structure of HCoV-HKU1 provides a high-quality model for group 2A CoVs, which are distinct from group 2B CoVs such as severe acute respiratory syndrome CoV. The structure, together with activity assays, supports the relative conservation at the P1 position that was discovered by sequencing the HCoV-HKU1 genome. Combined with structural data from other CoV M(pro)s, the HCoV-HKU1 M(pro) structure reported here provides insights into both substrate preference and the design of antivirals targeting CoVs.
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===Main protease of HCoV-HKU1===
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Structure of the main protease from a global infectious human coronavirus, HCoV-HKU1.,Zhao Q, Li S, Xue F, Zou Y, Chen C, Bartlam M, Rao Z J Virol. 2008 Sep;82(17):8647-55. Epub 2008 Jun 18. PMID:18562531<ref>PMID:18562531</ref>
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{{ABSTRACT_PUBMED_18562531}}
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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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==About this Structure==
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<div class="pdbe-citations 3d23" style="background-color:#fffaf0;"></div>
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[[3d23]] is a 4 chain structure of [[SARS Coronavirus Main Proteinase]] with sequence from [http://en.wikipedia.org/wiki/Unidentified_human_coronavirus Unidentified human coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D23 OCA].
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==See Also==
==See Also==
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*[[SARS Coronavirus Main Proteinase|SARS Coronavirus Main Proteinase]]
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*[[Virus protease 3D structures|Virus protease 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018562531</ref><references group="xtra"/>
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__TOC__
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[[Category: Unidentified human coronavirus]]
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</StructureSection>
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[[Category: Chen, C.]]
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[[Category: Large Structures]]
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[[Category: Li, S.]]
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[[Category: Synthetic construct]]
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[[Category: Zhao, Q.]]
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[[Category: Chen C]]
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[[Category: Zou, Y.]]
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[[Category: Li S]]
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[[Category: Atp-binding]]
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[[Category: Zhao Q]]
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[[Category: Endonuclease]]
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[[Category: Zou Y]]
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[[Category: Exonuclease]]
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[[Category: Helicase]]
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[[Category: Hydrolase]]
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[[Category: Main protease]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Nuclease]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleotidyltransferase]]
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[[Category: Protease]]
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[[Category: Rna replication]]
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[[Category: Rna-binding]]
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[[Category: Rna-directed rna polymerase]]
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[[Category: Thiol protease]]
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[[Category: Transferase]]
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[[Category: Transmembrane]]
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[[Category: Zinc-finger]]
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Current revision

Main protease of HCoV-HKU1

PDB ID 3d23

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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