1bfc

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(New page: 200px<br /> <applet load="1bfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfc, resolution 2.2&Aring;" /> '''BASIC FIBROBLAST GRO...)
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[[Image:1bfc.gif|left|200px]]<br />
 
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<applet load="1bfc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bfc, resolution 2.2&Aring;" />
 
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'''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT'''<br />
 
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==Overview==
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==BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT==
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Crystal structures of heparin-derived tetra- and hexasaccharides complexed, with basic fibroblast growth factor (bFGF) were determined at resolutions, of 1.9 and 2.2 angstroms, respectively. The heparin structure may be, approximated as a helical polymer with a disaccharide rotation of 174, degrees and a translation of 8.6 angstroms along the helix axis. Both, molecules bound similarly to a region of the bFGF surface containing, residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the, hexasaccharide also interacted with an additional binding site formed by, lysine-27, asparagine-102, and lysine-136. No significant conformational, change in bFGF occurred upon heparin oligosaccharide binding, which, suggests that heparin primarily serves to juxtapose components of the FGF, signal transduction pathway.
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<StructureSection load='1bfc' size='340' side='right'caption='[[1bfc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bfc]] is a 1 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=1BFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFC FirstGlance]. <br>
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</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>
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<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=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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfc OCA], [https://pdbe.org/1bfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfc RCSB], [https://www.ebi.ac.uk/pdbsum/1bfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bfc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1bfc ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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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]]
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1BFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BFC OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Heparin structure and interactions with basic fibroblast growth factor., Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC, Science. 1996 Feb 23;271(5252):1116-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8599088 8599088]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Faham, S.]]
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[[Category: Faham S]]
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[[Category: Rees, D.C.]]
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[[Category: Rees DC]]
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[[Category: growth factor]]
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[[Category: heparin-binding]]
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[[Category: mitogen]]
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[[Category: vascularization]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:09:12 2007''
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Current revision

BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT

PDB ID 1bfc

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