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Document Figure 9 Points of intervention for IL-1-based immunomodulation. Page 413 obtained from such studies can be imported into the available 3-dimensional structures. A combination of such structural insights coupled with the bioassay results provide clues leading to IL-1 functional information. In a previous structural report on IL-1β, we summarized the SDM results and identified a plausible receptor-binding epitope of interleukin-1 [42]. As mentioned before, electrostatic and hydrogen-bonding interactions in the loops between strands allow the polypeptide to adopt a conformation that enables an unusual concentration of polar and charged groups to be presented at the open end of the barrel. This cluster of charged residues forms an epitope with which IL-1 might bind to the receptor. Following our proposal, many groups have supported this hypothesis by employing mutagenesis studies. For a list of mutants and their activity results refer to References 42, 56, 59, and 61. Ju and coworkers are employing SDM to characterize interleukin-1 [55,56,58,61]. Substitution of Lys for the Asp145 of IL-β (D145K) greatly reduced agonist activity, while retaining 100% binding to the IL- 1RI [56]. Based on the sequence alignment of IL-1β with IL-1Ra, they selected Lys145 of IL-1Ra for mutagenesis and converted it to an aspartic acid. This mutant analog (IL-1Ra K145D) maintained receptor binding and gained partial agonist activity [56]. Following this study, Ju and coworkers selected five other amino acid residues in IL-1Ra for further analysis because the side chains of these residues appear to be in close proximity to Lys145 in IL-1Ra [61]. Mutations were made at Val18, Thr108, Cys116, Cys122, and Tyr147, usually by a replacement with the corresponding amino acid of IL-1β at each position. None of these muta- http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_413.html [4/5/2004 5:46:20 PM]
Document Figure 10 Schematic diagram showing the IL-1-based therapeutic molecules. Page 414 tions provided enough information related to the structure-activity relationship. The mutant IL-1Ra K145D was mutated further to V18S, T108K, C116F, C122S, C122A, Y147T, Y147G, H54P, and a H54I. Of these, K145D + T108K showed a 2-fold decrease in IL-1RI binding and a 3-fold decrease in bioactivity compared to the IL-1Ra K145D analog. The K145D + C116F combination resulted in the complete loss of bioactivity, whereas full receptor-binding activity was maintained. The observation that receptor-binding activity is preserved indicates that the binding site is not altered that much. Structural alignment http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_414.html (1 of 2) [4/5/2004 5:46:59 PM]
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Page 541 and 542: Document 17 Structure and Functiona
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Document D ddI, 152 tumour necrosis
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