Annual Review of Immunology Volume 27 2009 by Annual Reviews

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ANRV371-IY27-02 THE COMMON BETA CHAIN: βc βc is a type I transmembrane protein that serves as a shared signaling subunit for the receptors of IL-3, IL-5, and GM-CSF (Figure 1c and Figure 2a), which are related cytokines involved in the regulation of hematopoiesis and inflammation (82–84). Although βc does not measurably bind any of the ligands alone, its coexpression with cytokine-specific α receptors enhances the affinity of cytokine binding. The activated receptor complex, consisting of the cytokine ligand plus the α and βc receptors, initiates the intracellular signaling pathway mainly through JAK2 associated with the cytoplasmic domain of βc receptors (85).

Immunol. 27. org by University of Bergen UNIVERSITETSBIBLIOTEKET on 01/13/09. For personal use only. 20 Wang et al. In the absence of obvious conserved hotspot residues in γc -dependent cytokines, shape complementarity appears to play a dominant role. This assertion is supported by the observation that both IL-2 and IL-4 provide a shallow groove that accommodates the protruding hot-spot binding residues in γc . In IL-2, the bulky side chains from residues Thr-123, Qln126, Ser-127, Ile-129, and Ser-130 form the walls of a canyon, which receives a protruding ridge on γc composed of Tyr-103 and the Cys-160 to Cys-209 disulfide bond (Figure 8b).

The first one is composed of residue Tyr-103 from γc and residues Ser127 and Ser-130 from IL-2. In γc , the Tyr-103 side chain does not protrude outward toward IL-2 but is instead pinned back via a hydrogen bond with the Cys-209 main chain and is therefore positioned so that its aromatic ring packs flat against the side chains of Ser-127 and Ser-130 in IL-2 (Figure 8b). The second contact patch is around residue Gln-126 in IL-2, whose side chain is flattened and almost parallel to the surface formed by main chain atoms Annu.

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