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1fq9

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CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX

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Retrieved from "http://52.214.119.220/wiki/index.php/1fq9"

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-[[Image:1fq9.jpg|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX==
-|PDB= 1fq9 |SIZE=350|CAPTION= <scene name='initialview01'>1fq9</scene>, resolution 3.0&Aring;
+<StructureSection load='1fq9' size='340' side='right'caption='[[1fq9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=IDU:1,4-DIDEOXY-O2-SULFO-GLUCURONIC+ACID'>IDU</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=UAP:1,4-DIDEOXY-5-DEHYDRO-O2-SULFO-GLUCURONIC+ACID'>UAP</scene>
+<table><tr><td colspan='2'>[[1fq9]] is a 4 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=1FQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQ9 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=IDU:2-O-SULFO-BETA-L-ALTROPYRANURONIC+ACID'>IDU</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=UAP:4-DEOXY-2-O-SULFO-ALPHA-L-THREO-HEX-4-ENOPYRANURONIC+ACID'>UAP</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq9 OCA], [https://pdbe.org/1fq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fq9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fq9 ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1cvs|1CVS]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fq9 OCA], [http://www.ebi.ac.uk/pdbsum/1fq9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fq9 RCSB]</span>
+== 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/fq/1fq9_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1fq9 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX'''
+==See Also==
+*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
+*[[Fibroblast growth factor receptor 3D receptor|Fibroblast growth factor receptor 3D receptor]]
-==Overview==
+== References ==
-The crystal structure of a dimeric 2:2:2 FGF:FGFR:heparin ternary complex at 3 A resolution has been determined. Within each 1:1 FGF:FGFR complex, heparin makes numerous contacts with both FGF and FGFR, thereby augmenting FGF-FGFR binding. Heparin also interacts with FGFR in the adjoining 1:1 FGF:FGFR complex to promote FGFR dimerization. The 6-O-sulfate group of heparin plays a pivotal role in mediating both interactions. The unexpected stoichiometry of heparin binding in the structure led us to propose a revised model for FGFR dimerization. Biochemical data in support of this model are also presented. This model provides a structural basis for FGFR activation by small molecule heparin analogs and may facilitate the design of heparin mimetics capable of modulating FGF signaling.
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-FQ9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ9 OCA].
-==Reference==
-Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization., Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M, Mol Cell. 2000 Sep;6(3):743-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11030354 11030354]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Eliseenkova, A V.]]
+[[Category: Eliseenkova AV]]
-[[Category: Ibrahimi, O A.]]
+[[Category: Ibrahimi OA]]
-[[Category: Linhardt, R J.]]
+[[Category: Linhardt RJ]]
-[[Category: Mohammadi, M.]]
+[[Category: Mohammadi M]]
-[[Category: Plotnikov, A N.]]
+[[Category: Plotnikov AN]]
-[[Category: Schlessinger, J.]]
+[[Category: Schlessinger J]]
-[[Category: Yayon, A.]]
+[[Category: Yayon A]]
-[[Category: Yeh, B K.]]
+[[Category: Yeh BK]]
-[[Category: b-trefoil fold]]
-[[Category: i-set subgroup within the immunoglobulin superfamily]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:14 2008''

1fq9

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CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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