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  • Title: Heparin binds to the laminin alpha4 chain LG4 domain at a site different from that found for other laminins.
    Author: Yamashita H, Beck K, Kitagawa Y.
    Journal: J Mol Biol; 2004 Jan 30; 335(5):1145-9. PubMed ID: 14729333.
    Abstract:
    We previously reported that the LG4 domain of the laminin alpha4 chain is responsible for high-affinity heparin binding. To specify the amino acid residues involved in this activity, we produced a series of alpha4 LG4-fusion proteins in which each of the 27 basic residues (arginine, R; histidine; lysine, K) were replaced one by one with alanine (A). When the effective residues R1520A, K1531A, K1533A, and K1539A are mapped on a structural model, they form a track on the concave surface of the beta-sandwich, suggesting that they interact with adjacent sulfate groups along the heparin chain. Whereas low-affinity heparin-binding sites of other LG domains have been located at the top of the beta-sheet sandwich opposite the N and C termini, the residues for high-affinity heparin binding of alpha4 LG4 reveal a new topological area of the LG module.
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