ORF9b

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Betacoronavirus lipid binding protein
The X-ray crystallography structure of the SARS-CoV ORF9b protein dimer, showing the lipid molecule in the central cavity (yellow). From PDB: 2CME​.[1]
Identifiers
SymbolbCoV_lipid_BD
PfamPF09399
InterProIPR018542
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

ORF9b (formerly sometimes called ORF13) is a

amino acid residues long in SARS-CoV[2][3] and 98 in SARS-CoV-2,[4] in both cases forming a protein dimer
.

Nomenclature

There has been inconsistency in the nomenclature used for this gene in the scientific literature. In some work on SARS-CoV, it has been referred to as ORF13. It has also sometimes been referred to as ORF9a, resulting in a downstream ORF of 76

codons in SARS-CoV, also overlapping with the N gene, being designated ORF9b. The recommended nomenclature refers to the longer ORF as 9b and the downstream, shorter ORF as ORF9c.[5]

Structure

The ORF9b protein is 97

hydrophobic cavity in the center that binds lipids.[2][3][4] The lipid-binding cavity may serve as an unusual mechanism for anchoring the protein to membranes.[1]

A fragment of the SARS-CoV-2 ORF9b protein has been structurally characterized in a

Tom70 in which ORF9b forms an alpha helix rather than the beta-sheet structure observed in isolation.[6] This fold switching behavior is also consistent with bioinformatics predictions and may also occur for the SARS-CoV homolog.[7]

Expression and localization

ORF9b is one of two

In SARS-CoV, the protein is

Function

The function of the ORF9b protein is not well characterized. It is not essential for viral replication.[2]

Viral protein interactions

The ORF9b protein has been reported to interact with a number of other viral proteins, including

virions and thus may be a minor viral structural protein.[2][3][8]

Host cell effects

The ORF9b protein may be involved in modulating the host's

References

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