8YT8
Cryo-EM structure of the dystrophin glycoprotein complex
This is a non-PDB format compatible entry.
Summary for 8YT8
| Entry DOI | 10.2210/pdb8yt8/pdb |
| EMDB information | 39568 39569 |
| Descriptor | Alpha-sarcoglycan, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (18 entities in total) |
| Functional Keywords | complex membrane stability signaling, structural protein |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 9 |
| Total formula weight | 241238.93 |
| Authors | |
| Primary citation | Wan, L.,Ge, X.,Xu, Q.,Huang, G.,Yang, T.,Campbell, K.P.,Yan, Z.,Wu, J. Structure and assembly of the dystrophin glycoprotein complex. Nature, 637:1252-1260, 2025 Cited by PubMed Abstract: The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular matrix. Dysfunction of dystrophin and its associated proteins results in muscular dystrophy, a disorder characterized by progressive muscle weakness and degeneration. Despite the important roles of the DGC in physiology and pathology, its structural details remain largely unknown, hindering a comprehensive understanding of its assembly and function. Here we isolated the native DGC from mouse skeletal muscle and obtained its high-resolution structure. Our findings unveil a markedly divergent structure from the previous model of DGC assembly. Specifically, on the extracellular side, β-, γ- and δ-sarcoglycans co-fold to form a specialized, extracellular tower-like structure, which has a central role in complex assembly by providing binding sites for α-sarcoglycan and dystroglycan. In the transmembrane region, sarcoglycans and sarcospan flank and stabilize the single transmembrane helix of dystroglycan, rather than forming a subcomplex as previously proposed. On the intracellular side, sarcoglycans and dystroglycan engage in assembly with the dystrophin-dystrobrevin subcomplex through extensive interaction with the ZZ domain of dystrophin. Collectively, these findings enhance our understanding of the structural linkage across the cell membrane and provide a foundation for the molecular interpretation of many muscular dystrophy-related mutations. PubMed: 39663450DOI: 10.1038/s41586-024-08310-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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