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| == Structural insights == | | == Structural insights == |
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| The heparin binds in the dimer interface<ref>PMID:11276432</ref>. | | The heparin binds in the dimer interface<ref>PMID:18540049</ref>. |
| </StructureSection> | | </StructureSection> |
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Revision as of 01:49, 22 January 2016
FunctionFibroblast 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.
RelevanceFGF signaling is important in the pathogenesis of a variety of tumor types, angiogenesis and wound healing.
Structural insightsThe heparin binds in the dimer interface[2].
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3D structures of fibroblast growth factor3D structures of fibroblast growth factor
Updated on 22-January-2016
{"openlevels":0}
- FGF1
- 1fmm – FGF1 – Notophthalmus viridescens - NMR
- 1afc – bFGF1 + HS – bovine
- 1bar – bFGF1
- 2j3p – rFGF1 - rat
- 3hal – FGF1 - rabbit
- 2afg, 1jqz, 1rg8 – hFGF1 - human
- 1jt3, 1jt4, 1jt5, 1jt7, 1jtc, 1k5u, 1k5v, 1m16, 1jy0, 1nzk, 1p63, 1pzz, 1q03, 1q04, 1yto, 1z2v, 1z4s, 2aqz, 2hw9, 2hwa, 2hwm, 2hz9, 2ntd, 3b9u, 3ba4, 3ba5, 3ba7, 3bad, 3bag, 3bah, 3bao, 3baq, 3bau, 3bav, 3bb2, 2q9x, 3crg, 3crh, 3cri, 3cqa, 3fgm, 3fj8, 3fj9, 3fja, 3fjb, 3fjc, 3fjd, 3fje, 3fjf, 3fjh, 3fji, 3fjj, 3fjk, 3hom, 3o3q, 4q91, 4q9g, 4q9p, 4qal, 4qbc, 4qbv, 4qc4 – hFGF1 (mutant)
- 1dzd, 2rq9 – hFGF1 - NMR
- 1dzc – hFGF1 (mutant) - NMR
- FGF1 complex with small molecule
- 1axm, 2axm – hFGF1 + HS
- 3ud7, 3ud8, 3ud9, 3uda – hFGF1 + disaccharide
- 2uus – rFGF1 + HS
- 2erm – hFGF1 + HS - NMR
- 1rml – hFGF1 + naphthalene trisulphonate - NMR
- 1hkn – hFGF1 + naphthalene trisulphonate
- 2k8r – hFGF1 + anti-angiogenic drug - NMR
- 3k1x – hFGF1 + vasoprotectant drug
- 3jut – hFGF1 + inhibitor
- 2ki4, 2ki6 – hFGF1 + S100-A13
- FGF1 complex with FGF receptor
- 1e0o – hFGF1 (mutant) + hFGFR2 (mutant) + HS
- 3oj2, 3ojm, 1djs – hFGF1 + hFGFR2 (mutant)
- 1evt – hFGF1 + hFGFR1
- 3ojv – hFGF1 + hFGFR1 (mutant)
- 1ry7 – hFGF1 + hFGFR3
- 3cu1 – hFGF1 + hFGFR2
- 4j23 – hFGF1 + hFGFR2 + inhibitor
- FGF2
- 2fgf – hFGF2 precursor
- 1fga, 4fgf, 1bas, 1bfg, 2bfh, 1bff – hFGF2
- 1wvz, 2k43, 2k4a – hFGF2 - NMR
- 1bla, 1bld – hFGF2 (mutant) - NMR
- 1bfb, 1bfc – hFGF2 + heparin
- 1cvs – hFGF2 (mutant) + hFGFR1 (mutant)
- 1fq9 – hFGF2 (mutant) + hFGFR1 (mutant) + HS
- 1ev2 - hFGF2 (mutant) + hFGFR2
- 2m49 - hFGF2 (mutant) + S100-B
- 4oee, 4oef, 4oeg - hFGF2 (mutant) + disaccharide
- FGF4
- 1ijt – hFGF4 b-trefoil domain
- FGF7
- FGF8
- FGF9
- FGF10
- FGF12
- FGF13
- 3hbw – hFGF13
- 4dck – hFGF13 + calmodulin + sodium channel subunit α
- FGF18
- FGF19
- FGF20
- FGF23
ReferencesReferences
- ↑ Ornitz DM, Itoh N. Fibroblast growth factors. Genome Biol. 2001;2(3):REVIEWS3005. Epub 2001 Mar 9. PMID:11276432
- ↑ 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
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