Reovirus sigma C capsid protein, C-terminal (IPR007662)

Short name: SigmaC_C

Overlapping homologous superfamilies


Domain relationships



Protein sigmaC in its native state was shown to be a homotrimer. It was demonstrated that the sigmaC subunits are not covalently bound via disulphide linkages and the formation of an intrachain disulphide bond between the two cysteine residues of the sigmaC polypeptide may have a negative effect on oligomer stability. The susceptibility of the trimer to pH, temperature, ionic strength, chemical denaturants and detergents indicates that hydrophobic interactions contribute much more to oligomer stability than do ionic interactions and hydrogen bonding [PMID: 11752709].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.