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Fibroblast growth factor

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'''Fibroblast growth factors''' (FGF) are involved in angiogenesis, wound-healing and embryonic development. FGF is heparin-binding protein. FGF require heparan sulfate (HS) to activate the four FGF cell-surface receptors (FGFR). In vertebrates there are 23 members in the FGF family. FGF signaling is important in the pathogenesis of a variety of tumor types.<br />
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<StructureSection load='2uus' size='350' side='right' scene='' caption='Rat fibroblast growth factor 1 complex with heparan sulfate (PDB code [[2uus]]) '>
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== Function ==
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'''Fibroblast growth factors''' (FGF) are involved in angiogenesis, wound-healing and embryonic development. FGF is heparin-binding protein. FGF require heparan sulfate (HS) to activate the four FGF cell-surface receptors (FGFR). In vertebrates there are 23 members in the FGF family<ref>PMID:8747466</ref>. <br />
* '''FGF1''' is called acidic FGF.<br />
* '''FGF1''' is called acidic FGF.<br />
* '''FGF2''' is called basic FGF.<br />
* '''FGF2''' is called basic FGF.<br />
* '''FGF7''' is called keratinocyte growth factor which is present in the eiptheliazation-phase of wound healing when keratinocytes are covering the wound.
* '''FGF7''' is called keratinocyte growth factor which is present in the eiptheliazation-phase of wound healing when keratinocytes are covering the wound.
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== Relevance ==
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FGF signaling is important in the pathogenesis of a variety of tumor types.
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</StructureSection>
==3D structures of fibroblast growth factor==
==3D structures of fibroblast growth factor==
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**[[2p39]] – hFGF23 <br />
**[[2p39]] – hFGF23 <br />
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}}
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== References ==
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<references/>
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[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 22:25, 21 January 2016

Template:STRUCTURE 2uus


Rat fibroblast growth factor 1 complex with heparan sulfate (PDB code 2uus)

Drag the structure with the mouse to rotate

3D structures of fibroblast growth factor

Updated on 21-January-2016

References

  1. ↑ Athappilly FK, Hendrickson WA. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure. 1995 Dec 15;3(12):1407-19. PMID:8747466

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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