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Document Page 402 crystallography and heteronuclear NMR spectroscopy [40–49]. In addition to these, the structure of IL- 1β converting enzyme has been determined [50]. The molecule is an oligomeric cysteine protease consisting of 10- and 20-kDa subunits. To date proIL-1β is its only physiological substrate. As processing is essential for IL-1β extracellular transport and activity, inhibitors of ICE could provide a method to block the production of the active form of IL-1β. Although the elucidation of these structures have been important in determining various differences among the individual proteins, perhaps a more important result would be the elucidation of the structures of the two interleukin-1 receptor molecules, either individually or in complex with their substrates. This information could provide a means to draw together the present structural and biochemical knowledge into a coherent picture of the agonistic activity of IL-1α and IL-1β as opposed to the antagonist effect of IL-1Ra. The structures should also provide a foundation upon which structure-based drug design could proceed. To date no crystals or structural reports for the receptors have been published. A. The β-Trefoil Fold Structurally IL-1 exhibits a unique fold, known as a β-trefoil fold. Each IL-1 molecule show the characteristic β-trefoil fold and small deviations of the back-bone despite the relatively low sequence identity (Table 2). Figure 2 shows the structural alignment of the IL-1 molecules. The β-trefoil fold was first observed in Kunitz-type soybean trypsin inhibitor [51]. The fold has since been identified numerous times in the Kunitz family of protease inhibitors, the interleukin-1 system molecules, and the acidic and basic fibroblast growth factors [52]. Although these proteins have diverse biological function and low sequence identity to each other, all appear to have a common structural core. Each one, however, binds to its specific receptor with high affinity. The present known examples of proteins with such a fold are composed of between 125 and 170 amino acids. The overall fold itself is an antiparallel β barrel consisting of six two-stranded hairpins. Three of these form a barrel structure (strands denoted β1, β4, β5, β8, β9, and β12) while the other three are in a triangular array that caps the barrel. The arrangement of these moieties is such as to give the molecule a pseudo-three-fold axis [52]. Each fragment contributes one pair of antiparallel beta strands to the barrel and one pair to the cap of the barrel, thus forming a so called “open” and “closed” end to the structure [42]. B. Three-Dimensional Structure of IL-1β The structure of IL-1β was the first of the IL-1 family to be solved and has been solved independently five times: four times by x-ray crystallography [40– http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_402.html [4/5/2004 5:44:18 PM]
Document Figure 2 Structural alignment of IL-1α, IL-1β, and IL-1Ra. Residue numbering is taken from IL-1β. Residues bordered in black are conserved over the three molecules while those in gray constitute a conservative substitution. Arrows indicate sheet region, and the cylinders indicate helix. Figure produced by Stamp [109] and Alscript [110]. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_403.html [4/5/2004 5:44:25 PM] Page 403
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Page 541 and 542: Document 17 Structure and Functiona
Page 543 and 544: Document Table 1 Approval Indicatio
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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