1bfc: Difference between revisions

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New page: left|200px<br /> <applet load="1bfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfc, resolution 2.2Å" /> '''BASIC FIBROBLAST GRO...
 
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[[Image:1bfc.gif|left|200px]]<br />
<applet load="1bfc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bfc, resolution 2.2&Aring;" />
'''BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT'''<br />


==Overview==
==BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT==
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.
<StructureSection load='1bfc' size='340' side='right'caption='[[1bfc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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=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>
<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>
</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/bf/1bfc_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=1bfc ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
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]]
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
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]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Faham, S.]]
[[Category: Faham S]]
[[Category: Rees, D.C.]]
[[Category: Rees DC]]
[[Category: growth factor]]
[[Category: heparin-binding]]
[[Category: mitogen]]
[[Category: vascularization]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:09:12 2007''

Latest revision as of 06:35, 7 February 2024

BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT

1bfc, resolution 2.20Å

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