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10.15252/msb.202010079

http://scihub22266oqcxt.onion/10.15252/msb.202010079
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34519429!8438690!34519429
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suck abstract from ncbi


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pmid34519429      Mol+Syst+Biol 2021 ; 17 (9): e10079
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  • SARS-CoV-2 structural coverage map reveals viral protein assembly, mimicry, and hijacking mechanisms #MMPMID34519429
  • O'Donoghue SI; Schafferhans A; Sikta N; Stolte C; Kaur S; Ho BK; Anderson S; Procter JB; Dallago C; Bordin N; Adcock M; Rost B
  • Mol Syst Biol 2021[Sep]; 17 (9): e10079 PMID34519429show ga
  • We modeled 3D structures of all SARS-CoV-2 proteins, generating 2,060 models that span 69% of the viral proteome and provide details not available elsewhere. We found that 6% of the proteome mimicked human proteins, while 7% was implicated in hijacking mechanisms that reverse post-translational modifications, block host translation, and disable host defenses; a further 29% self-assembled into heteromeric states that provided insight into how the viral replication and translation complex forms. To make these 3D models more accessible, we devised a structural coverage map, a novel visualization method to show what is-and is not-known about the 3D structure of the viral proteome. We integrated the coverage map into an accompanying online resource (https://aquaria.ws/covid) that can be used to find and explore models corresponding to the 79 structural states identified in this work. The resulting Aquaria-COVID resource helps scientists use emerging structural data to understand the mechanisms underlying coronavirus infection and draws attention to the 31% of the viral proteome that remains structurally unknown or dark.
  • |*Protein Processing, Post-Translational[MESH]
  • |Amino Acid Transport Systems, Neutral/chemistry/genetics/metabolism[MESH]
  • |Angiotensin-Converting Enzyme 2/chemistry/genetics/*metabolism[MESH]
  • |Binding Sites[MESH]
  • |COVID-19/genetics/metabolism/virology[MESH]
  • |Computational Biology/methods[MESH]
  • |Coronavirus Envelope Proteins/chemistry/genetics/metabolism[MESH]
  • |Coronavirus Nucleocapsid Proteins/chemistry/genetics/metabolism[MESH]
  • |Host-Pathogen Interactions/*genetics[MESH]
  • |Humans[MESH]
  • |Mitochondrial Membrane Transport Proteins/chemistry/genetics/metabolism[MESH]
  • |Mitochondrial Precursor Protein Import Complex Proteins[MESH]
  • |Models, Molecular[MESH]
  • |Molecular Mimicry[MESH]
  • |Neuropilin-1/chemistry/genetics/metabolism[MESH]
  • |Phosphoproteins/chemistry/genetics/metabolism[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation, alpha-Helical[MESH]
  • |Protein Conformation, beta-Strand[MESH]
  • |Protein Interaction Domains and Motifs[MESH]
  • |Protein Interaction Mapping/methods[MESH]
  • |Protein Multimerization[MESH]
  • |SARS-CoV-2/chemistry/genetics/*metabolism[MESH]
  • |Spike Glycoprotein, Coronavirus/chemistry/genetics/*metabolism[MESH]
  • |Viral Matrix Proteins/chemistry/genetics/metabolism[MESH]
  • |Viroporin Proteins/chemistry/genetics/metabolism[MESH]


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