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Title | Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. |
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Journal, issue, pages | Nat Commun, Vol. 14, Page 2366-2366, Year 2023 |
Publish date | Jul 6, 2021 (structure data deposition date) |
Authors | Wydorski, P.M. / Osipiuk, J. / Lanham, B.T. / Tesar, C. / Endres, M. / Engle, E. / Jedrzejczak, R. / Mullapudi, V. / Michalska, K. / Fidelis, K. ...Wydorski, P.M. / Osipiuk, J. / Lanham, B.T. / Tesar, C. / Endres, M. / Engle, E. / Jedrzejczak, R. / Mullapudi, V. / Michalska, K. / Fidelis, K. / Fushman, D. / Joachimiak, A. / Joachimiak, L.A. |
External links | Nat Commun / PubMed:37185902 |
Methods | X-ray diffraction |
Resolution | 1.25 - 2.98 Å |
Structure data | PDB-7rbr: PDB-7rbs: PDB-7s6o: PDB-7s6p: PDB-7uv5: |
Chemicals | ChemComp-ZN: ChemComp-CL: ChemComp-EDO: ChemComp-HOH: ChemComp-ACT: |
Source |
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Keywords | HYDROLASE / covid-19 / coronavirus / SARS / CoV-2 / papain-like protease / ubiquitin / IDP51000 / IDP52003 / Center for Structural Genomics of Infectious Diseases / CSGID / ISG15 / SIGNALING PROTEIN / di-ubiquitin |