3snb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3snb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SNB FirstGlance]. <br> | <table><tr><td colspan='2'>[[3snb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SNB FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ECC:(4S)-4-AMINO-5-HYDROXYPENTANAMIDE'>ECC</scene></td></tr> | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ECC:(4S)-4-AMINO-5-HYDROXYPENTANAMIDE'>ECC</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h2z|2h2z]], [[3sn8|3sn8]], [[3sna|3sna]], [[3snc|3snc]], [[3snd|3snd]], [[3sne|3sne]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h2z|2h2z]], [[3sn8|3sn8]], [[3sna|3sna]], [[3snc|3snc]], [[3snd|3snd]], [[3sne|3sne]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3snb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3snb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3snb RCSB], [http://www.ebi.ac.uk/pdbsum/3snb PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3snb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3snb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3snb RCSB], [http://www.ebi.ac.uk/pdbsum/3snb PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease.,Zhu L, George S, Schmidt MF, Al-Gharabli SI, Rademann J, Hilgenfeld R Antiviral Res. 2011 Aug 11. PMID:21854807<ref>PMID:21854807</ref> | Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease.,Zhu L, George S, Schmidt MF, Al-Gharabli SI, Rademann J, Hilgenfeld R Antiviral Res. 2011 Aug 11. PMID:21854807<ref>PMID:21854807</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
| - | [[Category: Hilgenfeld, R | + | [[Category: Hilgenfeld, R]] |
| - | [[Category: Zhu, L | + | [[Category: Zhu, L]] |
[[Category: 3c-like proteinase]] | [[Category: 3c-like proteinase]] | ||
[[Category: Ac-dsfdq-h]] | [[Category: Ac-dsfdq-h]] | ||
Revision as of 15:25, 24 December 2014
Crystal structure of SARS coronavirus main protease complexed with Ac-DSFDQ-H (soaking)
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