| Description | Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and different pharmacological characteristics have been cloned from mouse and human cell lines: these have been termed type I and type II receptors []. The receptors both exist in transmembrane (TM) and soluble forms: the soluble IL-1 receptor is thought to be post-translationally derived from cleavage of the extracellular portion of the membrane receptors. Both IL-1 receptors appear to be well conserved in evolution, and map to the same chromosomal location []. The receptors can both bind all three forms of IL-1 (IL-1 alpha, IL-1 beta and interleukin-1 receptor antagonist, IL-1RA).The crystal structure of the soluble extracellular part of type-I IL1R complexed with IL1RA has been determined [ ]. The receptor structure is characterised by three Ig-like domains, of which domains 1 and 2 are tightly linked, while domain 3 is completely separate and connected by a flexible linker.This entry represents the interleukin-1 receptor family, which includes among others: interleukin-1 receptor type 1 (IL1R1), interleukin-1 receptor type 2 (IL1R2), interleukin-1 receptor accessory protein (IL1RAP), interleukin-18 receptor 1 and interleukin-18 receptor accessory protein. | Name | Interleukin-1 receptor family |
| Short Name | IL-1_rcpt_fam | Type | Family |
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