Summary for 9B8L
| Entry DOI | 10.2210/pdb9b8l/pdb |
| EMDB information | 44349 |
| Descriptor | Dysferlin (1 entity in total) |
| Functional Keywords | single-pass type ii membrane protein, membrane repair, calcium ion sensor, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 475154.19 |
| Authors | Huang, H.L.,Heissler, S.M.,Chinthalapudi, K. (deposition date: 2024-03-30, release date: 2024-11-27) |
| Primary citation | Huang, H.L.,Grandinetti, G.,Heissler, S.M.,Chinthalapudi, K. Cryo-EM structures of the membrane repair protein dysferlin. Nat Commun, 15:9650-9650, 2024 Cited by PubMed Abstract: Plasma membrane repair in response to damage is essential for cell viability. The ferlin family protein dysferlin plays a key role in Ca-dependent membrane repair in striated muscles. Mutations in dysferlin lead to a spectrum of diseases known as dysferlinopathies. The lack of a structure of dysferlin and other ferlin family members has impeded a mechanistic understanding of membrane repair mechanisms and the development of therapies. Here, we present the cryo-EM structures of the full-length human dysferlin monomer and homodimer at 2.96 Å and 4.65 Å resolution. These structures define the architecture of dysferlin, ferlin family-specific domains, and homodimerization mechanisms essential to function. Furthermore, biophysical and cell biology studies revealed how missense mutations in dysferlin contribute to disease mechanisms. In summary, our study provides a framework for the molecular mechanisms of dysferlin and the broader ferlin family, offering a foundation for the development of therapeutic strategies aimed at treating dysferlinopathies. PubMed: 39511170DOI: 10.1038/s41467-024-53773-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.65 Å) |
Structure validation
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