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Mode of Receptor Binding and Activation By Plasminogen-Related Growth Factors

  1. Author:
    Miller, M.
    Leonard, E. J.
    1. Year: 1998
  2. Journal: Febs Letters
    1. 429
    2. 1
    3. Pages: 1-3
  4. Type of Article: Article
  1. Abstract:

    Hepatocyte growth factor/scatter factor (HGF/SF) and macrophage stimulating protein (MSP) are plasminogen-related kringle proteins that lost serine protease domain enzymatic activity and became ligands for cell surface tyrosine kinase receptors. They are activated by cleavage to disulfide-linked ap chains. Surprisingly, despite structural similarities, the high affinity receptor binding regions of the two proteins are different: a chain for HGF, and beta chain for MSP. We propose that after cleavage exposes a beta chain binding site (high affinity for MSP, low affinity for HGF), monomeric ligand induces receptor dimerization and activation via alpha and beta chain binding sites of different affinity. (C) 1998 Federation of European Biochemical Societies. [References: 30]

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