1U2C
Crystal Structure of a-dystroglycan
Summary for 1U2C
| Entry DOI | 10.2210/pdb1u2c/pdb |
| Descriptor | Dystroglycan (2 entities in total) |
| Functional Keywords | ig-like domain, s6 like fold, protein binding |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Alpha-dystroglycan: Secreted, extracellular space (By similarity). Beta-dystroglycan: Cell membrane; Single- pass type I membrane protein (By similarity): Q62165 |
| Total number of polymer chains | 1 |
| Total formula weight | 26226.78 |
| Authors | Bozic, D.,Sciandra, F.,Lamba, D.,Brancaccio, A. (deposition date: 2004-07-18, release date: 2004-09-07, Last modification date: 2024-11-13) |
| Primary citation | Bozic, D.,Sciandra, F.,Lamba, D.,Brancaccio, A. The Structure of the N-terminal Region of Murine Skeletal Muscle {alpha}-Dystroglycan Discloses a Modular Architecture J.Biol.Chem., 279:44812-44816, 2004 Cited by PubMed 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. PubMed: 15326183DOI: 10.1074/jbc.C400353200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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