This domain can be found in leukemia inhibitory factor receptor (LIFR). LIFR is a cell surface receptor that mediates the actions of LIF and other interleukin-6 type cytokines through the formation of signalling complexes with gp130. This is the N-terminal domain, referred to as domain 1, which contains conserved disulfide bonds between Cys-10 to Cys-20 and Cys-37 to Cys-45 [].
On the basis of functional and structural similarities, the small cytokines leukemia inhibitory factor (LIF) and oncostatin (OSM) can be classified into a single family [, ].It has been said []that LIF and OSM can be included in the IL-6 family of cytokines, but while all these cytokines seem to be structurally related, the sequence similarity is not high enough to allow the use of a single consensus pattern.
On the basis of functional and structural similarities, the small cytokines leukemia inhibitory factor (LIF) and oncostatin (OSM) can be classified into a single family [, ].It has been said []that LIF and OSM can be included in the IL-6 family of cytokines, but while all these cytokines seem to be structurally related, the sequence similarity is not high enough to allow the use of a single consensus pattern.The signature pattern for this entry is based on a conserved region in the C-terminal region. This region is centred on a conserved cysteine which has been shown, in OSM, to be involved in a disulphide bond [].
