3m3v
From Proteopedia
(Difference between revisions)
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<StructureSection load='3m3v' size='340' side='right'caption='[[3m3v]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3m3v' size='340' side='right'caption='[[3m3v]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3m3v]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3m3v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M3V FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ea8|3ea8]], [[3ea7|3ea7]], [[3e91|3e91]], [[3m3s|3m3s]], [[3m3t|3m3t]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ea8|3ea8]], [[3ea7|3ea7]], [[3e91|3e91]], [[3m3s|3m3s]], [[3m3t|3m3t]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3v OCA], [https://pdbe.org/3m3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m3v RCSB], [https://www.ebi.ac.uk/pdbsum/3m3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m3v ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/R1A_CVHSA R1A_CVHSA]] The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> The main proteinase 3CL-PRO is 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 (By similarity). Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> Nsp9 is a ssRNA-binding protein.<ref>PMID:17024178</ref> <ref>PMID:17692280</ref> <ref>PMID:19369340</ref> |
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Virus protease 3D structures|Virus protease 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:32, 20 July 2022
SARS-CoV main protease triple mutant STI/A with two N-terminal additional residue (Gly-Ser)
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