The cytokine structural homologs IL-1β and IL-1Ra have distinct dynamical character that potentially influence their roles in allosteric regulation of the IL-1 receptor.
Interleukin-1{beta} (IL-1{beta}) and the interleukin-1 receptor antagonist (IL-1Ra) share the {beta}-trefoil fold, engage the same receptor (IL-1R), but produce opposite biological outcomes. IL-1{beta} recruits the accessory protein IL-1RAcP to initiate inflammatory signaling while IL-1Ra occupies the receptor without supporting co-receptor recruitment. Seeking the origin of this divergence in…
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