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J. Biol. Chem., Vol. 269, Issue 17, 12874-12879, Apr, 1994

X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution

GP Vigers, P Caffes, RJ Evans, RC Thompson, SP Eisenberg and BJ Brandhuber
Synergen, Inc., Boulder, Colorado 80301.

Interleukin-1 receptor antagonist (IL-1ra) is a natural competitive antagonist of IL-1. In order to further elucidate the mechanism by which IL-1ra binds without activating the IL-1 receptor, we have solved the crystal structure of IL-1ra at 2.0-A resolution. IL-1ra has the same overall beta-trefoil fold as IL-1 alpha and IL-1 beta and has a very similar hydrophobic core. However, there are a number of structural differences between the molecules, including significant differences at the open end of the beta-barrel, which has been identified in IL-1 beta as a receptor binding site.
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