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Document Table 2 RMS Distance of Aligned Cα Moieties of the Three Interleukin-1 Structures IL-1β IL-1α IL-1Ra IL-1β 0.0 1.8 Å (36.3%) 1.42 Å (30.7%) IL-1α 1.8 Å (36.3%) 0.0 1.8 Å (27.5%) IL-1Ra 1.42 Å (30.7%) 1.8 Å (27.5%) 0.0 Number in parentheses referred to sequence identities between the aligned structures. A. Expression and Processing of IL-1 Page 399 All three IL-1 molecules, IL-1α, IL-1β, and IL-1Ra are synthesized as 31 kDa precursor molecules produced primarily by mononuclear phagocytes. These precursor proteins can be subsequently processed to mature 17 kDa molecules. The means whereby this is achieved appears to be different for each type of molecule and may help to explain the roles of the three. Both agonist molecules IL-1α and IL-1β lack a classical hydrophobic leader sequence and thus must be processed in an alternative way. The two can be separated by their biological activity in the precursor form, IL-1α being active in both precursor and mature forms while IL-1β produces a biological response only in its processed form. In addition, a specific enzyme, Interleukin-1 beta converting enzyme (ICE), cleaves IL-1β to its mature form. This enzyme is a cysteine protease whose only known substrate is proIL-1β, which it cleaves at Ala 117 [19,20]. The means whereby pro IL-1α is processed is still largely a mystery although it has been postulated that a calpain or related protein may perform the task. Naturally occurring IL-1Ra is a 22 kDa glycosylated protein [14,15,21– 24] that possesses a signal sequence. It is likely that it is processed in the conventional manner as can be concluded by the glycosylation states of the molecule not present in the agonists [25]. The LPS-stimulated human blood monocytes initially express the gene for IL-1Ra [25]. An alternatively spliced form of IL-1Ra also exists (intracellular IL-1Ra), which remains inside the cell presumably to block intracellular IL-1 action [26]. Both soluble and intracellular forms of IL-1Ra block IL-1R but do not trigger any biological response. B. Receptors and Responses http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_399.html (1 of 2) [4/5/2004 5:44:09 PM]
Document All effects of the IL-1 family are exerted via their receptors, which are present on a variety of different cell types. There are two known IL-1 receptors. The first, type I (IL-1RI) is an 80-kDa formation found mainly on T cells and fibroblasts; the second, type II (IL-1RII) is present on B cells, monocytes, neutrophils, and heptoma cells and is approximately 60 kDa in size. From sequence analysis these molecules are believed to belong to the Ig-superfamily, the extracellular portion of the receptors consisting of three immunoglobulin-like domains of approximately 100 residues each [27,28]. The IL- 1RI receptor http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_399.html (2 of 2) [4/5/2004 5:44:09 PM]
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Structure-based Drug Design 14 Stru
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Document D ddI, 152 tumour necrosis
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