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[[Image:1ev2.jpg|left|200px]]<br /><applet load="1ev2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ev2, resolution 2.20&Aring;" />
'''CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2)==
To elucidate the structural determinants governing specificity in, fibroblast growth factor (FGF) signaling, we have determined the crystal, structures of FGF1 and FGF2 complexed with the ligand binding domains, (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1), and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between, D2-D3) interfaces define a general binding site for all FGF-FGFR, complexes. Specificity is achieved through interactions between the, N-terminal and central regions of FGFs and two loop regions in D3 that are, subject to alternative splicing. These structures provide a molecular, basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR, specificity through primary sequence variations and alternative splicing.
<StructureSection load='1ev2' size='340' side='right'caption='[[1ev2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ev2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EV2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ev2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ev2 OCA], [https://pdbe.org/1ev2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ev2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ev2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ev2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FGF2_HUMAN FGF2_HUMAN] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.<ref>PMID:1721615</ref> <ref>PMID:8663044</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ev/1ev2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ev2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
To elucidate the structural determinants governing specificity in fibroblast growth factor (FGF) signaling, we have determined the crystal structures of FGF1 and FGF2 complexed with the ligand binding domains (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1) and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between D2-D3) interfaces define a general binding site for all FGF-FGFR complexes. Specificity is achieved through interactions between the N-terminal and central regions of FGFs and two loop regions in D3 that are subject to alternative splicing. These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing.


==Disease==
Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity.,Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M Cell. 2000 May 12;101(4):413-24. PMID:10830168<ref>PMID:10830168</ref>
Known diseases associated with this structure: Hypophosphatemic rickets, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]], Osteomalacia, tumor-induced OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605380 605380]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1EV2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV2 OCA].
</div>
<div class="pdbe-citations 1ev2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity., Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M, Cell. 2000 May 12;101(4):413-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10830168 10830168]
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
*[[Fibroblast growth factor receptor 3D receptor|Fibroblast growth factor receptor 3D receptor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hubbard, S.R.]]
[[Category: Hubbard SR]]
[[Category: Mohammadi, M.]]
[[Category: Mohammadi M]]
[[Category: Plotnikov, A.N.]]
[[Category: Plotnikov AN]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger J]]
[[Category: SO4]]
[[Category: b-trefoil fold]]
[[Category: immunoglobulin (ig)like domains belonging to the i-set subgroup within ig-like domains]]
 
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