| Literature DB >> 8175703 |
G P Vigers1, P Caffes, R J Evans, R C Thompson, S P Eisenberg, B J Brandhuber.
Abstract
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.Entities:
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Year: 1994 PMID： 8175703
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157