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New page: left|200px<br /> <applet load="2fgf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fgf, resolution 1.77Å" /> '''THREE-DIMENSIONAL S...
 
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[[Image:2fgf.gif|left|200px]]<br />
<applet load="2fgf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2fgf, resolution 1.77&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA'''<br />


==Overview==
==THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA==
The three-dimensional structure of the 146-residue form of human basic, fibroblast growth factor (bFGF), expressed as a recombinant protein in, yeast, has been determined by x-ray crystallography to a resolution of 1.8, A. bFGF is composed entirely of beta-sheet structure, comprising a, three-fold repeat of a four-stranded antiparallel beta-meander. The, topology of bFGF is identical to that of interleukin 1 beta, showing that, although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally, related mitogenic factors. Analysis of the three-dimensional structure in, light of functional studies of bFGF suggests that the receptor binding, site and the positively charged heparin binding site correspond to, adjacent but separate loci on the beta-barrel.
<StructureSection load='2fgf' size='340' side='right'caption='[[2fgf]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fgf]] 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=2FGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FGF 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]] 1.77&#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=2fgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgf OCA], [https://pdbe.org/2fgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fgf RCSB], [https://www.ebi.ac.uk/pdbsum/2fgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fgf 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/fg/2fgf_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=2fgf 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/>
2FGF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FGF OCA].
__TOC__
 
</StructureSection>
==Reference==
Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta., Zhang JD, Cousens LS, Barr PJ, Sprang SR, Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3446-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1849658 1849658]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Sprang, S.R.]]
[[Category: Sprang SR]]
[[Category: Zhang, J.]]
[[Category: Zhang J]]
[[Category: SO4]]
[[Category: growth factor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:05:02 2007''

Latest revision as of 09:23, 14 February 2024

THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA

2fgf, resolution 1.77Å

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