Fibroblast growth factor: Difference between revisions

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== Structural insights ==
== Structural insights ==


The heparin binds in the dimer interface<ref>PMID:11276432</ref>.  
The heparin binds in the dimer interface<ref>PMID:18540049</ref>.  
</StructureSection>
</StructureSection>



Revision as of 01:49, 22 January 2016

Function

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[1].

  • FGF1 is called acidic FGF.
  • FGF2 is called basic FGF.
  • FGF7 is called keratinocyte growth factor which is present in the eiptheliazation-phase of wound healing when keratinocytes are covering the wound.

Relevance

FGF signaling is important in the pathogenesis of a variety of tumor types, angiogenesis and wound healing.

Structural insights

The heparin binds in the dimer interface[2].

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 factor3D structures of fibroblast growth factor

Updated on 22-January-2016

ReferencesReferences

  1. Ornitz DM, Itoh N. Fibroblast growth factors. Genome Biol. 2001;2(3):REVIEWS3005. Epub 2001 Mar 9. PMID:11276432
  2. Kulahin N, Kiselyov V, Kochoyan A, Kristensen O, Kastrup JS, Berezin V, Bock E, Gajhede M. Dimerization effect of sucrose octasulfate on rat FGF1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):448-52. Epub 2008 May 16. PMID:18540049 doi:10.1107/S174430910801066X

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky