Hepatocyte growth factor: Difference between revisions

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Michal Harel, Alexander Berchansky

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 <StructureSection load='1shy' size='350' side='right' caption='Structure of human HGF β chain (grey) complex with HGF receptor Sema and ψ domains (green) (PDB entry [[1shy]])' scene=''>
 == Function ==
-'''Hepatocyte growth factor''' (HGF) regulates cell growth, motility and morphogenesis.  HGF binds to proto-oncogene c-Met receptor and activates a tyrosine kinase signaling cascade.  HGF precursor is cleaved by serine protease to α (69 kD) and β (34 kD) chains which form a disulfide bond to produce the active heterodimer<ref>PMID:1838014</ref>.  HGF α chain contains an N-terminal hairpin and 4 kringle domains.  The kringle domain participates in protein-protein interaction and its structure is of a large loop which is stabilized by 3 Cys-Cys bonds.  HGF β chain is catalytically inactive serine protease-like.  '''HGF NK1''' - a natural splice variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF<ref>PMID:9488442</ref>.  '''HGF NK2''' variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF.
+'''Hepatocyte growth factor''' (HGF) regulates cell growth, motility and morphogenesis.  HGF binds to proto-oncogene c-Met receptor and activates a tyrosine kinase signaling cascade.  HGF precursor is cleaved by serine protease to α (69 kD) and β (34 kD) chains which form a disulfide bond to produce the active heterodimer<ref>PMID:1838014</ref>.  '''HGF α chain''' contains an N-terminal hairpin and 4 kringle domains.  The kringle domain participates in protein-protein interaction and its structure is of a large loop which is stabilized by 3 Cys-Cys bonds.  '''HGF β chain''' is catalytically inactive serine protease-like.  '''HGF NK1''' - a natural splice variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF<ref>PMID:9488442</ref>.  '''HGF NK2''' variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF.
 == Relevance ==