title: Structure of the activating IL-1 receptor signaling complex.
abstract: Interleukin-1 (IL-1)-family cytokines are mediators of innate and adaptive immunity. They exert proinflammatory effects by binding a primary receptor that recruits a receptor accessory protein to form a signaling-competent heterotrimeric complex. Here we present the crystal structure of IL-1β bound to its primary receptor IL-1RI and its receptor accessory protein IL-1RAcP, providing insight into how IL-1-type cytokines initiate signaling and revealing an evolutionary relationship with the fibroblast growth factor receptor family.
authors.affiliation: Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California, USA.
authors.forename: Christoph
authors.initials: C
authors.lastname: Thomas
authors.forename: J Fernando
authors.initials: JF
authors.lastname: Bazan
authors.forename: K Christopher
authors.initials: KC
authors.lastname: Garcia
mesh_terms: D018360:Crystallography, X-Ray; D006801:Humans; D053577:Interleukin-1 Receptor Accessory Protein / Q000737:chemistry* / Q000378:metabolism; D053583:Interleukin-1beta / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D053573:Receptors, Interleukin-1 Type I / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D053577:Interleukin-1 Receptor Accessory Protein; D053583:Interleukin-1beta; D053573:Receptors, Interleukin-1 Type I