Dystroglycan (DG) is a cell-surface laminin receptor. In skeletal muscle it is a central component of the dystrophin-glycoprotein (DGC) complex (Ervasti & Campbell 1991). Mutations in components of the DGC render muscle fibres more susceptible to damage and lead to various types of muscle disorder such as Duchenne muscular dystrophy and limb-girdle muscular dystrophies (Straub & Campbell, 1997, Cohn & Campbell 2000). DG is present as non-covalently associated alpha and beta subunits following cleavage at Ser654. The extracellular alpha subunit binds to laminin-2 (merosin) in the muscle basement membrane while the membrane-associated beta subunit binds dystrophin, which associates with the actin cytoskeleton (Ervasti & Campbell 1993, Yamada et al. 1994, Talts et al. 1999). Alpha-DG also binds the carboxy-terminal G domains of laminin alpha-1 (Gee et al. 1993, Zhou et al. 2012) and alpha-5 (Yu & Talts 2003). G domains are relatively well conserved in all five alpha-laminin chains, so DG is likely to bind all laminin heterotrimers.