8dmk | pdb_00008dmk

Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies

spinqualitylabelsall models 8dmk, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dmk is a 3 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.7Å Ligands: CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LAMA1_MOUSE Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Publication Abstract from PubMed 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 A structure of the trimeric laminin polymer node containing alpha1, beta1 and gamma1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease. Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies.,Kulczyk AW, McKee KK, Zhang X, Bizukojc I, Yu YQ, Yurchenco PD Nat Commun. 2023 Jan 19;14(1):317. doi: 10.1038/s41467-023-36077-z. PMID:36658135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laminin

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