Hepatocyte growth factor

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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=''>
<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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== Function ==
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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 (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. See also [[Hepatocyte growth factor receptor]].
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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.
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== Relevance ==
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High levels of HGF are associated with liver diseases<ref>PMID:7806142</ref>, lung diseases, acute cardiac infraction, vascular diseases, renal failure, neurologic diseases like Alzheimer Disease, pancreatic diseases, several types of cancer and diabetes type II<ref>PMID:19154948</ref><ref>PMID:7806142</ref>. HGF administration can reverse liver chirrosis<ref>PMID:12482615</ref>.
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</StructureSection>
==3D structures of hepatocyte growth factor==
==3D structures of hepatocyte growth factor==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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===HGF N terminal===
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*HGF full length 1-728
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[[2hgf]] – hHGF N terminal – human - NMR <br />
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**[[7mo7]], [[7mo8]], [[7mo9]], [[7moa]], [[7mob]] – hHGF + hHGFR – human – Cryo EM <br />
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[[3hms]], [[3hmt]] – hHGF N terminal <br />
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[[3hmr]] – mHGF N terminal – mouse <br />
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===HGF NK1 variant===
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*HGF N terminal 28-126
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[[1bht]], [[1nk1]], [[1gp9]], [[2qj2]], [[2qj4]] – hHGF NK1 <br />
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**[[2hgf]] – hHGF N terminal – human - NMR <br />
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[[1gmn]], [[1gmo]], [[3mkp]] – hHGF NK1 (mutant) + heparin<br />
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**[[3hms]], [[3hmt]] – hHGF N terminal <br />
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**[[3hmr]] – mHGF N terminal – mouse <br />
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===HGF NK2 variant===
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*HGF NK1 variant 28-210
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[[3hn4]] – hHGF NK2 <br />
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**[[1bht]], [[1gp9]], [[1nk1]], [[2qj2]], [[2qj4]] – hHGF NK1 <br />
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[[3sp8]] – hHGF NK2 (mutant) + heparin<br />
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**[[5coe]], [[5cs1]], [[5cs5]], [[5cs9]] – hHGF NK1 (mutant) <br />
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[[4iua]] – mHGF NK2 (mutant) <br />
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**[[1gmn]], [[1gmo]], [[3mkp]] – hHGF NK1 (mutant) + heparin<br />
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**[[5cp9]], [[5ct1]], [[5ct2]], [[5ct3]], [[5cs3]], [[5csq]] – hHGF NK1 (mutant) + inhibitor<br />
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**[[4d3c]] – hHGF NK1 (mutant) + antibody<br />
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===HGF β chain===
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*HGF NK2 variant 28-289
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[[1si5]] – hHGF β chain (mutant) <br />
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**[[3hn4]] – hHGF NK2 <br />
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[[1shy]] – hHGF β chain (mutant) + HGF receptor Sema and ψ domains<br />
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**[[3sp8]] – hHGF NK2 (mutant) + heparin<br />
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**[[4iua]] – mHGF NK2 (mutant) <br />
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===HGF α+β chain===
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* HGF α chain (69 kD) 495-728
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**[[1si5]] – hHGF α chain (mutant) <br />
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**[[1shy]] – hHGF α chain (mutant) + HGF receptor Sema and ψ domains<br />
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*HGF β chain 25-567
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**[[4o3t]], [[4o3u]] – hHGF β chain (mutant) + HGF receptor Sema and ψ domains + zymogen activator peptide<br />
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*HGF α+β chain
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**[[4k3j]] – hHGF α (mutant) + β + antibody <br />
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**[[6lz9]] – hHGF α (mutant) + K4 domain 388-494 + antibody <br />
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}}
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== References ==
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<references/>
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[[4k3j]] – hHGF α (mutant) + β + antibody <br />
 
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

3D structures of hepatocyte growth factor

Updated on 25-August-2025

References

  1. ↑ Nakamura T. Structure and function of hepatocyte growth factor. Prog Growth Factor Res. 1991;3(1):67-85. PMID:1838014
  2. ↑ Jakubczak JL, LaRochelle WJ, Merlino G. NK1, a natural splice variant of hepatocyte growth factor/scatter factor, is a partial agonist in vivo. Mol Cell Biol. 1998 Mar;18(3):1275-83. PMID:9488442
  3. ↑ Shiota G, Okano J, Kawasaki H, Kawamoto T, Nakamura T. Serum hepatocyte growth factor levels in liver diseases: clinical implications. Hepatology. 1995 Jan;21(1):106-12. PMID:7806142
  4. ↑ Anan F, Masaki T, Yonemochi H, Takahashi N, Nakagawa M, Eshima N, Saikawa T, Yoshimatsu H. Hepatocyte growth factor levels are associated with the results of 123I-metaiodobenzylguanidine myocardial scintigraphy in patients with type 2 diabetes mellitus. Metabolism. 2009 Feb;58(2):167-73. doi: 10.1016/j.metabol.2008.09.009. PMID:19154948 doi:http://dx.doi.org/10.1016/j.metabol.2008.09.009
  5. ↑ Shiota G, Okano J, Kawasaki H, Kawamoto T, Nakamura T. Serum hepatocyte growth factor levels in liver diseases: clinical implications. Hepatology. 1995 Jan;21(1):106-12. PMID:7806142
  6. ↑ Funakoshi H, Nakamura T. Hepatocyte growth factor: from diagnosis to clinical applications. Clin Chim Acta. 2003 Jan;327(1-2):1-23. PMID:12482615

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