Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kulczyk AW, McKee KK, Zhang X, Bizukojc I, Yu YQ, Yurchenco PD. Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies. Nat Commun. 2023 Jan 19;14(1):317. doi: 10.1038/s41467-023-36077-z. PMID:36658135 doi:http://dx.doi.org/10.1038/s41467-023-36077-z
