A high affinity hepatocyte growth factor-binding site in the immunoglobulin-like region of Met.

ABSTRACT: Hepatocyte growth factor (HGF) and its high affinity receptor, the tyrosine kinase Met, play a key role in embryo development and tumor invasion. Both HGF and Met are established targets for cancer therapy. However, the mechanism of their interaction is complex and remains elusive. HGF is secreted as a monomeric precursor (pro-HGF) that binds to but does not activate Met. Mature HGF is a alpha/beta heterodimer containing a high affinity Met-binding site in the alpha-chain (HGF-alpha) and a low affinity Met-binding site in the beta-chain (HGF-beta). The extracellular portion of Met contains a semaphorin (Sema) domain, a cysteine-rich hinge (plexin-semaphorin-integrin), and four immunoglobulin-like domains (immunoglobulin-like regions in plexins and transcription factors (IPT) 1-4). HGF-beta

SUBMITTER: Basilico C 

PROVIDER: S-EPMC2475716 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature