7T2T
SARS-CoV2 Mpro native form
Summary for 7T2T
| Entry DOI | 10.2210/pdb7t2t/pdb |
| Descriptor | 3C-like proteinase (2 entities in total) |
| Functional Keywords | sars-cov2, 3c-like protease, mpro, 2clpro, hydrolase |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
| Total number of polymer chains | 1 |
| Total formula weight | 33825.55 |
| Authors | Mathews, I.I.,Hameedi, M.A.,Wakatsuki, S. (deposition date: 2021-12-06, release date: 2022-09-14, Last modification date: 2023-10-18) |
| Primary citation | Hameedi, M.A.,T Prates, E.,Garvin, M.R.,Mathews, I.I.,Amos, B.K.,Demerdash, O.,Bechthold, M.,Iyer, M.,Rahighi, S.,Kneller, D.W.,Kovalevsky, A.,Irle, S.,Vuong, V.Q.,Mitchell, J.C.,Labbe, A.,Galanie, S.,Wakatsuki, S.,Jacobson, D. Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro. Nat Commun, 13:5285-5285, 2022 Cited by PubMed Abstract: In addition to its essential role in viral polyprotein processing, the SARS-CoV-2 3C-like protease (3CLpro) can cleave human immune signaling proteins, like NF-κB Essential Modulator (NEMO) and deregulate the host immune response. Here, in vitro assays show that SARS-CoV-2 3CLpro cleaves NEMO with fine-tuned efficiency. Analysis of the 2.50 Å resolution crystal structure of 3CLpro C145S bound to NEMO reveals subsites that tolerate a range of viral and host substrates through main chain hydrogen bonds while also enforcing specificity using side chain hydrogen bonds and hydrophobic contacts. Machine learning- and physics-based computational methods predict that variation in key binding residues of 3CLpro-NEMO helps explain the high fitness of SARS-CoV-2 in humans. We posit that cleavage of NEMO is an important piece of information to be accounted for, in the pathology of COVID-19. PubMed: 36075915DOI: 10.1038/s41467-022-32922-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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