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7JTL

Structure of SARS-CoV-2 ORF8 accessory protein

Summary for 7JTL
Entry DOI10.2210/pdb7jtl/pdb
DescriptorORF8 protein, SODIUM ION (3 entities in total)
Functional Keywordssars-cov-2, sars2, covid-19, coronavirus, accessory protein, host-factor restriction, rna virus, immune evasion, mhc-i, open reading frame 8, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
Total number of polymer chains2
Total formula weight24470.73
Authors
Flower, T.G.,Buffalo, C.Z.,Hooy, R.M.,Allaire, M.,Ren, X.,Hurley, J.H. (deposition date: 2020-08-18, release date: 2020-08-26, Last modification date: 2024-10-09)
Primary citationFlower, T.G.,Buffalo, C.Z.,Hooy, R.M.,Allaire, M.,Ren, X.,Hurley, J.H.
Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein.
Proc.Natl.Acad.Sci.USA, 118:-, 2021
Cited by
PubMed Abstract: The molecular basis for the severity and rapid spread of the COVID-19 disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely unknown. ORF8 is a rapidly evolving accessory protein that has been proposed to interfere with immune responses. The crystal structure of SARS-CoV-2 ORF8 was determined at 2.04-Å resolution by X-ray crystallography. The structure reveals a ∼60-residue core similar to SARS-CoV-2 ORF7a, with the addition of two dimerization interfaces unique to SARS-CoV-2 ORF8. A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, YIDI Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities.
PubMed: 33361333
DOI: 10.1073/pnas.2021785118
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.04 Å)
Structure validation

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