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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Crystallography, X-Ray
-
Humans
-
Interleukin-1 Receptor Accessory Protein / chemistry*
-
Interleukin-1 Receptor Accessory Protein / metabolism
-
Interleukin-1beta / chemistry*
-
Interleukin-1beta / metabolism
-
Models, Molecular
-
Protein Conformation
-
Receptors, Interleukin-1 Type I / chemistry*
-
Receptors, Interleukin-1 Type I / metabolism
-
Signal Transduction
Substances
-
Interleukin-1 Receptor Accessory Protein
-
Interleukin-1beta
-
Receptors, Interleukin-1 Type I