Hepatocyte growth factor

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(New page: <StructureSection load='1shy' size='350' side='right' caption='Structure of human HGF β chain complex with HGF receptor Sema and ψ domains (PDB entry 1shy)' scene=''> '''Hepatocyte...)
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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=''>
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<StructureSection load='1shy' size='350' side='right' caption='Structure of human HGF β chain complex with HGF receptor Sema and ψ domains (PDB entry [[1shy]])' scene=''>
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'''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 and β (residues 495-728) chains which form a disulfide bond to produce the active heterodimer. HGF NK1 variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF. 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 and β (residues 495-728) chains which form a disulfide bond to produce the active heterodimer. HGF NK1 variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF. HGF NK2 variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF.

Revision as of 10:50, 12 May 2013

Structure of human HGF β chain (grey) complex with HGF receptor Sema and ψ domains (green) (PDB entry 1shy)

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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