v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This OB-fold domain folds into a five-stranded β-barrel [ ]. Proteins containing this domain are found in various staphylococcal toxins described as staphylococcal superantigen-like (SSL) proteins that are related to the staphylococcal enterotoxins (SEs) or superantigens. These SSL proteins of which 11 have so far been characterised have a typical SE tertiary structure consisting of a distinct oligonucleotide/oligosaccharide binding (OB-fold), this domain, linked to a β-grasp domain, family Stap_Strp_tox_C (). SSLs do not bind to T-cell receptors or major histocompatibility complex class II molecules and do not stimulate T cells. SSLs target components of innate immunity, such as complement, Fc receptors, and myeloid cells [, , , , , , ]. SSL protein 7 (SSL7) is the best characterised of the SSLs and binds complement factor C5 and IgA with high affinity and inhibits the end stage of complement activation and IgA binding to FcgammaR []. |
| Short Name | SSL_OB |