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Fig. 2. DGC and dystroglycan ligands. Schematic representation of dystroglycan within the DGC. Structural domains of dystroglycan-binding proteins are represented in the insets. Domains of dystrophin described in the text are represented. A similar domain structure is found in utrophin. ${alpha}$ -Dystrobrevin lacks a WW domain but contains the EF-hand and ZZ domains. Laminins are composed of three distinct chains termed ${alpha}$ , ß and ${gamma}$ . To date, 5 ${alpha}$ , 4 ß and 3 ${gamma}$ laminin chains have been identified that can combine to form 15 different isoforms (Hallmann et al., 2005). In the C-terminal ends of the ${alpha}$ chains, there are globular G domains (LG 1-5) composed of five similar modules. Dystroglycan binds with high affinity to the LG domains of laminin 1 ( ${alpha}$ 1ß1 ${gamma}$ 1) and 2 ( ${alpha}$ 2ß1 ${gamma}$ 1) ${alpha}$ chains (Talts et al., 1999). Antibodies against the C-terminal LG4-LG5 pair of the ${alpha}$ 1 chain (E3 fragment) have been widely used for organ morphogenesis studies.

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