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Document Figure 1 Schematic representations of the members of the IL-1 family. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_400.html [4/5/2004 5:44:15 PM] Page 400
Document has a single membrane-spanning region and a cytoplasmic region of 213 amino acids. The IL-1RII receptor has a single membrane-spanning region and a cytoplasmic region of 29 amino acids. Page 401 All three IL-1 molecules bind with a high affinity to the receptor IL-1RI. However only IL-1α and IL- 1β produce a detectable response [29]. The IL-1Ra molecule completely blocks the binding of the former two molecules without inducing any signal transduction events. The second IL-1 receptor, IL- 1RII, similarly binds IL-1 tightly but does not produce any signal [30]. The soluble portion of IL-1RI binds to IL-1Ra, IL-1α, and IL-1β in decreasing order of affinity whereas the soluble portion of IL-1RII binds IL-1β, proIL-1β, IL-1α, and IL-1Ra, in that order. It therefore appears that both IL-1Ra and IL- 1RII take part in modulation of the agonist molecules, an argument supported <strong>by</strong> the finding that soluble IL-1RII binds IL-1β with a similar affinity to the cell-associated receptor; whereas, the affinity of IL- 1Ra to such a soluble receptor is some 2000 times less [31,32,33]. Greenfeder, et al., [18] have identified a new molecule, the IL-1 accessory protein IL-1RacP. The complex of IL-1 and IL-1 receptor binds to IL-1RacP and together they induce the signal [18]. Greenfeder also observed that antibodies to IL-1RI and to IL-1RacP block IL-1 binding and activity. From sequence analysis it appears that the cytoplasmic domains of IL-1R and IL-1RacP contain the same amino acid domains commonly found in the members of the GTPase family of proteins [34]. It has been proposed that such a complexation may lead to a closer proximity of these cytoplasmic domains and thus facilitate signal transduction. A scheme showing functional relationships between molecules that make up the IL-1 system—IL-1α, IL-1β, IL- 1Ra, IL-1RI, IL-1RII, and related receptors—is shown in Figure 1. C. Autoantibodies of IL-1 In addition to these molecules, naturally occurring neutralizing autoantibodies of IgG type to IL-1α have been identified. These have been detected in serum isolated from human donors. [35,36]. These antibodies bind to both proIL-1α and 17-kDa IL-1α [37] and completely prevent the binding of IL-1α to type-I cell surface receptors [38]. Patients with autoimmune diseases have higher populations of these antibodies [39]. III. Three-Dimensional Structural Information In an effort to understand the natural and interactions of the IL-1 family, various laboratories have undertaken the task of elucidating the three-dimensional structure of the molecules. To the present this has resulted in the structures of all three members of the IL-1 family being solved independently <strong>by</strong> both x-ray http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_401.html [4/5/2004 5:44:16 PM]
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Structure-based Drug Design 14 Stru
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Document Page 108 mulate during tre
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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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