Low nidogen affinity of laminin‐5 can be attributed to two serine residues in EGF‐like motif γ2III4

@article{Mayer1995LowNA,
  title={Low nidogen affinity of laminin‐5 can be attributed to two serine residues in EGF‐like motif $\gamma$2III4},
  author={Ulrike Mayer and Ernst Pöschl and Donald R. Gerecke and D. Wolfe Wagman and Robert E. Burgeson and Rupert Dr. Timpl},
  journal={FEBS Letters},
  year={1995},
  volume={365}
}
High affinity nidogen binding of laminin‐1 (chain composition α1β1γ1) has been previously mapped to a single EGF‐like motif γ1III4 of its γ1 chain. Two more isoforms, laminin‐5 (α3β3γ2) and laminin‐7 (α3β2γ1), show low and high binding activity, respectively, indicating that the γ2 chain is of low affinity. This was confirmed by recombinant production of the homologous EGF‐like motif γ2III4 of the γ2 chain, which has a 100,000‐fold lower binding activity than γ1III4. The crucial heptapeptide… Expand
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