Abstract
Dystroglycan (DG) is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellular and highly glycosylated, and beta-dystroglycan, spanning the cell membrane. It is a pivotal member of the dystrophin-glycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors. We report the 2.3-A resolution crystal structure of the murine skeletal muscle N-terminal alpha-DG region, which confirms the presence of two autonomous domains; the first finally identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. Solid-phase laminin binding assays show the occurrence of protein-protein type of interactions involving the Ig-like domain of alpha-DG.
Highlights
Dystroglycan (DG) is a cell surface receptor consisting of two subunits: ␣-dystroglycan, extracellular and highly glycosylated, and -dystroglycan, spanning the cell membrane
It is a pivotal member of the dystrophinglycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors
We report the 2.3-Å resolution crystal structure of the murine skeletal muscle N-terminal ␣-DG region, which confirms the presence of two autonomous domains; the first identified as an Ig-like and the second resembling ribosomal RNA-binding proteins
Summary
Dystroglycan (DG)1 [1], earlier identified as cranin [2], is a type-1 transmembrane protein expressed in muscle as well as in a wide variety of other tissues [3]. We report the 2.3-Å resolution crystal structure of the murine skeletal muscle N-terminal ␣-DG region, which confirms the presence of two autonomous domains; the first identified as an Ig-like and the second resembling ribosomal RNA-binding proteins.
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