FGFAcidic and basic fibroblast growth factor family. |
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| SMART accession number: | SM00442 |
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| Description: | Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities. |
| Interpro abstract (IPR002348): | The interleukin-1 (IL1) and heparin-binding growth factor (HBGF) families share low sequence similarity (about 25% [(PUBMED:1849658)]) but have very similar structures. Coupled with the Kunitz-type soybean trypsin inhibitors (STI), they form a structural superfamily. Despite their structural correspondence, however, they show no sequence similarity to the STI family. The crystal structures of interleukin-1 beta and HBGF1 have been solved, showing both families to have the same 12-stranded beta-sheet structure [(PUBMED:1738162)]; the beta-sheets are arranged in 3 similar lobes around a central axis, 6 strands forming an anti-parallel beta-barrel [(PUBMED:1707542), (PUBMED:4071057)]. The beta-sheets are generally well preserved and the crystal structures superimpose in these areas. The intervening loops are less well conserved - the loop between beta-strands 6 and 7 is slightly longer in interleukin-1 beta. |
| GO function: | growth factor activity (GO:0008083) |
| Family alignment: |
There are 772 FGF domains in 772 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Go to specific node: Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes - Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Wilkie AO, Morriss-Kay GM, Jones EY, Heath JK
- Functions of fibroblast growth factors and their receptors.
- Curr Biol. 1995; 5: 500-7
- Display abstract
Fibroblast growth factors were first characterized twenty years ago as mitogens of cultured fibroblasts. Despite a wealth of data from experiments in vitro, insights have begun to emerge only recently on the normal function of these growth factors in mice and humans, as a result of studies of natural and experimental mutations in the factors and their receptors.
- Yamaguchi TP, Rossant J
- Fibroblast growth factors in mammalian development.
- Curr Opin Genet Dev. 1995; 5: 485-91
- Display abstract
Polypeptide growth factors are secreted signalling molecules that function as intercellular communicators. Detailed analyses of the expression and function of members of the fibroblast growth factor (FGF) family and their recepotors have demonstrated that the FGF signalling pathways play essential roles in regulating cellular proliferation, differentiation and tissue patterning during vertebrate embryogenesis. Recent studies on the molecular basis of human dysmorphic syndromes have revealed that aberrant FGF signalling during limb and skeletal development can lead to pathogenesis.
- Baird A
- Fibroblast growth factors: activities and significance of non-neurotrophin neurotrophic growth factors.
- Curr Opin Neurobiol. 1994; 4: 78-86
- Display abstract
Although first characterized by virtue of their ability to stimulate endothelial cell proliferation in vitro and angiogenesis in vivo, the fibroblast growth factors are now also well recognized for their neurotrophic activities. Understanding the physiological significance of these multifunctional, virtually ubiquitous and pluripotential molecules, however, remains enigmatic. Recent advances describing their molecular, biochemical and biological characteristics has led to a better understanding of their role in the central nervous system.
- Mason IJ
- The ins and outs of fibroblast growth factors.
- Cell. 1994; 78: 547-52
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 33.33 map04810 Regulation of actin cytoskeleton 33.33 map04010 MAPK signaling pathway 33.33 map05218 Melanoma This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with FGF domain which could be assigned to a KEGG orthologous group, and not all proteins containing FGF domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of FGF domains in PDB
PDB code Main view Title 1afc 
Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor 1axm 
Heparin-linked biologically-active dimer of fibroblast growth factor 1bar 
Three-dimensional structures of acidic and basic fibroblast growth factors 1bas 
Three-dimensional structures of acidic and basic fibroblast growth factors 1bfb 
Basic fibroblast growth factor complexed with heparin tetramer fragment 1bfc 
Basic fibroblast growth factor complexed with heparin hexamer fragment 1bff 
The 154 amino acid form of human basic fibroblast growth factor 1bfg 
Crystal structure of basic fibroblast growth factor at 1.6 angstroms resolution 1bla 
Basic fibroblast growth factor (fgf-2) mutant with cys 78 replaced by ser and cys 96 replaced by ser, nmr 1bld 
Basic fibroblast growth factor (fgf-2) mutant with cys 78 replaced by ser and cys 96 replaced by ser, nmr 1cvs 
Crystal structure of a dimeric fgf2-fgfr1 complex 1djs 
Ligand-binding portion of fibroblast growth factor receptor in complex with fgf1 1dzc 
High resolution structure of acidic fibroblast growth factor. mutant fgf-4-ala-(23-154), 24 nmr structures 1dzd 
High resolution structure of acidic fibroblast growth factor (27-154), 24 nmr structures 1e0o 
Crystal structure of a ternary fgf1-fgfr2-heparin complex 1ev2 
Crystal structure of fgf2 in complex with the extracellular ligand binding domain of fgf receptor 2 (fgfr2) 1evt 
Crystal structure of fgf1 in complex with the extracellular ligand binding domain of fgf receptor 1 (fgfr1) 1fga 
Refinement of the structure of human basic fibroblast growth factor at 1.6 angstroms resolution and analysis of presumed heparin binding sites by selenate substitution 1fmm 
Solution structure of nfgf-1 1fq9 
Crystal structure of a ternary fgf2-fgfr1-heparin complex 1g82 
Structure of fibroblast growth factor 9 1hkn 
A complex between acidic fibroblast growth factor and 5-amino-2-naphthalenesulfonate 1ihk 
Crystal structure of fibroblast growth factor 9 (fgf9) 1ii4 
Crystal structure of ser252trp apert mutant fgf receptor 2 (fgfr2) in complex with fgf2 1iil 
Crystal structure of pro253arg apert mutant fgf receptor 2 (fgfr2) in complex with fgf2 1ijt 
Crystal structure of fibroblast growth factor 4 (fgf4) 1jqz 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag. 1jt3 
Human acidic fibroblast growth factor. 141 amino acid form with amino histidine tag and leu 73 replaced by val (l73v) 1jt4 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and val 109 replaced by leu (v109l) 1jt5 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 73 replaced by val and val 109 replaced by leu (l73v/v109l) 1jt7 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced by phe and leu 73 replaced by val and val 109 replaced by leu (l44f/l73v/v109l) 1jtc 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced by phe (l44f) 1jy0 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and cys 117 replaced with val (c117v). 1k5u 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag with his93 replaced by gly (h93g). 1k5v 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag with asn106 replaced by gly (n106g). 1m16 
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced with phe (l44f), leu 73 replaced with val (l73v), val 109 replaced with leu (v109l) and cys 117 replaced with val (c117v). 1nun 
Crystal structure analysis of the fgf10-fgfr2b complex 1nzk 
Crystal structure of a multiple mutant (l44f, l73v, v109l, l111i, c117v) of human acidic fibroblast growth factor 1p63 
Human acidic fibroblast growth factor. 140 amino acid form with amino terminal his tag and leu111 replaced with ile (l111i) 1pwa 
Crystal structure of fibroblast growth factor 19 1pzz 
Crystal structure of fgf-1, v51n mutant 1q03 
Crystal structure of fgf-1, s50g/v51g mutant 1q04 
Crystal structure of fgf-1, s50e/v51n 1q1u 
Crystal structure of human fhf1b (fgf12b) 1qqk 
The crystal structure of fibroblast growth factor 7 (keratinocyte growth factor) 1qql 
The crystal structure of fibroblast growth factor 7/1 chimera 1rg8 
Human acidic fibroblast growth factor (hafgf-1) at 1.10 angstrom resolution (140 amino acid form) 1rml 
Nmr study of acid fibroblast growth factor bound to 1,3,6- naphthalene trisulphonate, 26 structures 1ry7 
Crystal structure of the 3 ig form of fgfr3c in complex with fgf1 1yto 
Crystal structure of gly19 deletion mutant of human acidic fibroblast growth factor 1z2v 
Crystal structure of glu60 deletion mutant of human acidic fibroblast growth factor 1z4s 
Crystal structure of gly19 and glu60 deletion mutant of human acidic fibroblast growth factor 2afg 
2.0 angstrom x-ray structure of human acidic fibroblast growth factor 2aqz 
Crystal structure of fgf-1, s17t/n18t/g19 deletion mutant 2axm 
Heparin-linked biologically-active dimer of fibroblast growth factor 2bfh 
Crystal structure of basic fibroblast growth factor at 1.6 angstroms resolution 2erm 
Solution structure of a biologically active human fgf-1 monomer, complexed to a hexasaccharide heparin-analogue 2fdb 
Crystal structure of fibroblast growth factor (fgf)8b in complex with fgf receptor (fgfr) 2c 2fgf 
Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1beta 2hw9 
Crystal structure of lys12cys/cys117val mutant of human acidic fibroblast growth factor at 1.60 angstrom resolution. 2hwa 
Crystal structure of lys12thr/cys117val mutant of human acidic fibroblast growth factor at 1.65 angstrom resolution. 2hwm 
Crystal structure of lys12val/cys117val mutant of human acidic fibroblast growth factor at 1.60 angstrom resolution 2hz9 
Crystal structure of lys12val/asn95val/cys117val mutant of human acidic fibroblast growth factor at 1.70 angstrom resolution. 2j3p 
Crystal structure of rat fgf1 at 1.4 a 2k43 
Acidic fibroblast growth factor solution structure in the fgf-1-c2a binary complex: key component in the fibroblast growthfactor non-classical pathway 2k4a 
Fgf-1-c2a binary complex structure: a key component in the fibroblast growthfactor non-classical pathway 2k8r 
Solution structure of human acidic fibroblast growth factor in complex with anti-angiogenic drug inositol hexaphosphate (ip6) 2ntd 
Human fibroblast growth factor-1 (140 amino acid form) with cys117val/pro134cys mutations 2p23 
Crystal structure of human fgf19 2p39 
Crystal structure of human fgf23 2q9x 
Crystal structure of highly stable mutant q40p/s47i/h93g of human fibroblast growth factor-1 2uus 
Crystal structure of the rat fgf1-sucrose octasulfate (sos) complex. 3b9u 
Crystal structure of l26n/d28n/h93g mutant of human acidic fibroblast growth factor 3ba4 
Crystal structure of l26d mutant of human acidic fibroblast growth factor 3ba5 
Crystal structure of d28a mutant of human acidic fibroblast growth factor 3ba7 
Crystal structure of l26n/d28a mutant of human acidic fibroblast growth factor 3bad 
Crystal structure of d70a/h93g mutant of human acidic fibroblast growth factor 3bag 
Crystal structure of k112n/n114a mutant of human acidic fibroblast growth factor 3bah 
Crystal structure of k112n mutant of human acidic fibroblast growth factor 3bao 
Crystal structure of l26n mutant of human acidic fibroblast growth factor 3baq 
Crystal structure of l26a mutant of human acidic fibroblast growth factor 3bau 
Crystal structure of k12v/l26d/d28a mutant of human acidic fibroblast growth factor 3bav 
Crystal structure of l26a/d28n mutant of human acidic fibroblast growth factor 3bb2 
Crystal structure of l26d/d28n mutant of human acidic fibroblast growth factor 3cqa 
Crystal structure of human fibroblast growth factor-1 with mutations glu81ala and lys101ala 3crg 
Crystal structure of human fibroblast growth factor-1 with mutations glu81ala, glu82asn and lys101ala 3crh 
Crystal structure of human fibroblast growth factor-1 with mutations glu81ser and lys101ala 3cri 
Crystal structure of human fibroblast growth factor-1 with mutations glu81ser, glu82asn and lys101ala 3cu1 
Crystal structure of 2:2:2 fgfr2d2:fgf1:sos complex 3f1r 
Crystal structure of fgf20 dimer 3fgm 
Crystal structure of l44f/c83t/c117v/f132w mutant of human acidic fibroblast growth factor 3fj8 
Crystal structure of c117i mutant of human acidic fibroblast growth factor 3fj9 
Crystal structure of f85w mutant of human acidic fibroblast growth factor 3fja 
Crystal structure of f132w mutant of human acidic fibroblast growth factor 3fjb 
Crystal structure of v31i mutant of human acidic fibroblast growth factor 3fjc 
Crystal structure of l44w mutant of human acidic fibroblast growth factor 3fjd 
Crystal structure of l44f/f132w mutant of human acidic fibroblast growth factor 3fje 
Crystal structure of c83s mutant of human acidic fibroblast growth factor 3fjf 
Crystal structure of c83t mutant of human acidic fibroblast growth factor 3fjh 
Crystal structure of c83a mutant of human acidic fibroblast growth factor 3fji 
Crystal structure of k12v/c83i/c117v mutant of human acidic fibroblast growth factor 3fjj 
Crystal structure of c83v mutant of human acidic fibroblast growth factor 3fjk 
Crystal structure of a66c mutant of human acidic fibroblast growth factor 3hbw 
Crystal structure of human fibroblast growth factor homologous factor 2a (fhf2a), also referred to as fibroblast growth factor 13a (fgf13a) 3hom 
Crystal structure of oxidized a66c mutant of human acidic fibroblast growth factor 4fgf 
Refinement of the structure of human basic fibroblast growth factor at 1.6 angstroms resolution and analysis of presumed heparin binding sites by selenate substitution - Links (links to other resources describing this domain)
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PFAM FGF INTERPRO IPR002348 PROSITE HBGF_FGF