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Updated: Aug 13, 2025

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies
Arkadiusz W Kulczyk1, Karen K McKee2, Ximo Zhang3
1Institute for Quantitative Biomedicine, Department of Biochemistry and Microbiology, Rutgers University, Piscataway, NJ, 08854, USA. arek.kulczyk@rutgers.edu.
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.
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