8ysa

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(New page: '''Unreleased structure''' The entry 8ysa is ON HOLD Authors: Zheng, W.Y., Fu, L.F., Feng, Y., Han, P., Qi, J.X. Description: The co-crystal structure of SARS-CoV-2 Mpro in complex wit...)
Current revision (08:41, 9 May 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8ysa is ON HOLD
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==The co-crystal structure of SARS-CoV-2 Mpro in complex with compound H102==
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<StructureSection load='8ysa' size='340' side='right'caption='[[8ysa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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Authors: Zheng, W.Y., Fu, L.F., Feng, Y., Han, P., Qi, J.X.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ysa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2] 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=8YSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YSA FirstGlance]. <br>
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Description: The co-crystal structure of SARS-CoV-2 Mpro in complex with compound H102
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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]] 1.5&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=ELL:(2S)-2-azanyl-3-[(3S)-2-oxidanylidenepyrrolidin-3-yl]propanal'>ELL</scene>, <scene name='pdbligand=TBG:3-METHYL-L-VALINE'>TBG</scene></td></tr>
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[[Category: Qi, J.X]]
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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=8ysa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ysa OCA], [https://pdbe.org/8ysa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ysa RCSB], [https://www.ebi.ac.uk/pdbsum/8ysa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ysa ProSAT]</span></td></tr>
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[[Category: Zheng, W.Y]]
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</table>
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[[Category: Fu, L.F]]
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== Function ==
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[[Category: Han, P]]
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[https://www.uniprot.org/uniprot/R1A_SARS2 R1A_SARS2] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7]
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[[Category: Feng, Y]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Severe acute respiratory syndrome coronavirus 2]]
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[[Category: Synthetic construct]]
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[[Category: Feng Y]]
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[[Category: Fu LF]]
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[[Category: Han P]]
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[[Category: Qi JX]]
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[[Category: Zheng WY]]

Current revision

The co-crystal structure of SARS-CoV-2 Mpro in complex with compound H102

PDB ID 8ysa

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