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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.