The Structure of the N-terminal Region of Murine Skeletal Muscle α-Dystroglycan Discloses a Modular Architecture
Dystroglycan (DG) is a cell surface receptor consisting of two subunits: α-dystroglycan, extracellular and highly glycosylated, and β-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 proc...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-10, Vol.279 (43), p.44812 |
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| container_issue | 43 |
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| container_title | The Journal of biological chemistry |
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| creator | Damir Bozic Francesca Sciandra Doriano Lamba Andrea Brancaccio |
| description | Dystroglycan (DG) is a cell surface receptor consisting of two subunits: α-dystroglycan, extracellular and highly glycosylated,
and β-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-Ã
resolution crystal structure of the murine skeletal muscle N-terminal α-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 α-DG. |
| doi_str_mv | 10.1074/jbc.C400353200 |
| format | Article |
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and β-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-Ã
resolution crystal structure of the murine skeletal muscle N-terminal α-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
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and β-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-Ã
resolution crystal structure of the murine skeletal muscle N-terminal α-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
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and β-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-Ã
resolution crystal structure of the murine skeletal muscle N-terminal α-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 α-DG.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15326183</pmid><doi>10.1074/jbc.C400353200</doi></addata></record> |
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| ispartof | The Journal of biological chemistry, 2004-10, Vol.279 (43), p.44812 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_highwire_biochem_279_43_44812 |
| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| title | The Structure of the N-terminal Region of Murine Skeletal Muscle α-Dystroglycan Discloses a Modular Architecture |
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