Determinants of laminin polymerization revealed by the structure of the α5 chain amino‐terminal region
Determinants of laminin polymerization revealed by the structure of the α5 chain amino‐terminal region
The polymerization of laminin into a cell‐associated network—a key step in basement membrane assembly—is mediated by the laminin amino‐terminal (LN) domains at the tips of the three short arms of the laminin αβγ‐heterotrimer. The crystal structure of a laminin α5LN–LE1–2 fragment shows that the LN domain is a β‐jelly roll with several elaborate insertions that is attached like a flower head to the stalk‐like laminin‐type epidermal growth factor‐like tandem. A surface loop that is strictly conserved in the LN domains of all α‐short arms is required for stable ternary association with the β‐ and γ‐short arms in the laminin network.
- Imperial College London United Kingdom
Models, Molecular, Binding Sites, Scientific Reports, Molecular Sequence Data, 540, Basement Membrane, Polymerization, Protein Structure, Tertiary, Mice, Animals, Amino Acid Sequence, Laminin, Protein Multimerization, Protein Structure, Quaternary, Protein Binding
Models, Molecular, Binding Sites, Scientific Reports, Molecular Sequence Data, 540, Basement Membrane, Polymerization, Protein Structure, Tertiary, Mice, Animals, Amino Acid Sequence, Laminin, Protein Multimerization, Protein Structure, Quaternary, Protein Binding
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