8 forms a homodimer

Stable Identifier
R-HSA-9755354
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
ReviewStatus
5/5
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Structural studies have revealed that SARS-CoV-2 ORF8 (8) protein forms a homodimer and adopts an Ig-like fold. Two novel SARS-CoV-2-specific dimerization interfaces have been identified. The covalent dimer interface is formed by intermolecular disulfide bridge between Cys20 of each monomer. In addition, a separate noncovalent interface is formed by the SARS-CoV-2-specific YIDI motif (residues 73-76) (Flower TG et al. 2021).
Literature References
PubMed ID Title Journal Year
33361333 Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein

Flower, TG, Hurley, JH, Ren, X, Hooy, RM, Allaire, M, Buffalo, CZ

Proc Natl Acad Sci U S A 2021
Participants
Participates
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
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Reviewed
Created
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