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Mode of receptor binding and activation by plasminogen‐related growth factors 1
Author(s) -
Miller Maria,
Leonard Edward J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00533-x
Subject(s) - hepatocyte growth factor , chemistry , kringle domain , receptor , serine protease , cleavage (geology) , biochemistry , serine , ligand (biochemistry) , receptor tyrosine kinase , protease , enzyme , biology , plasmin , fracture (geology) , paleontology
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 αβ chains. Surprisingly, despite structural similarities, the high affinity receptor binding regions of the two proteins are different: α chain for HGF, and β chain for MSP. We propose that after cleavage exposes a β chain binding site (high affinity for MSP, low affinity for HGF), monomeric ligand induces receptor dimerization and activation via α and β chain binding sites of different affinity.