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. Author manuscript; available in PMC: 2022 May 21.
Published in final edited form as: Matrix Biol. 2021 May 21;98:49–63. doi: 10.1016/j.matbio.2021.05.004

Figure 1. Laminin-111 assembly, protein domains and LN-LEa segments.

Figure 1.

A. Model of laminin polymerization based on previous studies. Laminin first assembles into a β-γ dimer through LN domain interactions. The α-LN domain of a third laminin molecule binds to the β-γ dimer in a calcium-dependent interaction, forming the polymer node. Additional laminin molecules bind to the initial complex, forming a sheet-like polymer (cc, critical concentration of polymerization). B. Domain organization of laminin-111 with corresponding LN-LEa segments. C. Coomassie Blue-stained gel (SDS-PAGE, 7.5%, reduced) of recombinant. α1-, β1- and γ1-LN-LEa glycoproteins. D. PNGaseF de-glycosylation of α1-LN-LEa. After enzyme treatment, a single band, migrating at 55 kDa, is seen.