8DMK
Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies
Summary for 8DMK
| Entry DOI | 10.2210/pdb8dmk/pdb |
| EMDB information | 27542 |
| Descriptor | Laminin subunit alpha-1, Laminin subunit beta-1, Laminin subunit gamma-1, ... (5 entities in total) |
| Functional Keywords | laminin, complex, basement membrane, structural protein |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 3 |
| Total formula weight | 105058.05 |
| Authors | Kulczyk, A.W. (deposition date: 2022-07-08, release date: 2023-02-01, Last modification date: 2024-11-06) |
| Primary citation | Kulczyk, A.W.,McKee, K.K.,Zhang, X.,Bizukojc, I.,Yu, Y.Q.,Yurchenco, P.D. Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies. Nat Commun, 14:317-317, 2023 Cited by PubMed Abstract: Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron microscopy to determine a 3.7 Å structure of the trimeric laminin polymer node containing α1, β1 and γ1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. PubMed: 36658135DOI: 10.1038/s41467-023-36077-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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