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TitleUbiquitin variants potently inhibit SARS-CoV-2 PLpro and viral replication via a novel site distal to the protease active site.
Journal, issue, pagesPlos Pathog., Vol. 18, Page e1011065-e1011065, Year 2022
Publish dateMay 20, 2022 (structure data deposition date)
Authorsvan Vliet, V.J.E. / Huynh, N. / Pala, J. / Patel, A. / Singer, A. / Slater, C. / Chung, J. / van Huizen, M. / Teyra, J. / Miersch, S. ...van Vliet, V.J.E. / Huynh, N. / Pala, J. / Patel, A. / Singer, A. / Slater, C. / Chung, J. / van Huizen, M. / Teyra, J. / Miersch, S. / Luu, G.K. / Ye, W. / Sharma, N. / Ganaie, S.S. / Russell, R. / Chen, C. / Maynard, M. / Amarasinghe, G.K. / Mark, B.L. / Kikkert, M. / Sidhu, S.S.
External linksPlos Pathog. / PubMed:36548304
MethodsX-ray diffraction
Resolution3.5 Å
Structure data

PDB-8cx9:
Structure of the SARS-COV2 PLpro (C111S) in complex with a dimeric Ubv that inhibits activity by an unusual allosteric mechanism
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-BR:
BROMIDE ION

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/SIGNALING PROTEIN / inhibitor complex / allosteric inhibition / VIRAL PROTEIN / VIRAL PROTEIN-SIGNALING PROTEIN complex

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