| First Author | Bozic D | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 43 | Pages | 44812-6 |
| PubMed ID | 15326183 | Mgi Jnum | J:93985 |
| Mgi Id | MGI:3510490 | Doi | 10.1074/jbc.C400353200 |
| Citation | Bozic D, et al. (2004) The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture. J Biol Chem 279(43):44812-6 |
| abstractText | 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. |
