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New page: left|200px<br /> <applet load="1bfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bfg, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1bfg.gif|left|200px]]<br />
<applet load="1bfg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bfg, resolution 1.6&Aring;" />
'''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION==
We have determined the crystal structures of two types of human basic, fibroblast growth factor, the serine analogue and the wild-type, at 1.6, and 2.5 A resolution, respectively. Two good heavy atom derivatives were, found and used for multiple isomorphous replacement phasing. The atomic, coordinates were refined using the Hendrickson &amp; Konnert program for, stereochemically restrained refinement against structure factors. The, crystallographic R factors were reduced to 15.3% for the serine analogue, structure and 16.0% for the wild-type structure. The serine analogue and, wild-type structures have been found to be almost identical, the, root-mean-square deviation between the corresponding C alpha atoms being, 0.11 A. Their structures are composed of twelve beta-strands forming a, barrel and three loops. Their molecules have an approximate threefold, internal symmetry and are similar in architecture to that of interleukin-1, beta. A possible heparin-binding site, which comprises five basic, residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by, calculating the electrostatic potential energy.
<StructureSection load='1bfg' size='340' side='right'caption='[[1bfg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bfg]] 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=1BFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFG 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]] 1.6&#8491;</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=1bfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfg OCA], [https://pdbe.org/1bfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfg RCSB], [https://www.ebi.ac.uk/pdbsum/1bfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfg 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/1bfg_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=1bfg 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]]
*[[Cation-pi interactions|Cation-pi interactions]]
 
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
==About this Structure==
== References ==
1BFG 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=1BFG OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem (Tokyo). 1991 Sep;110(3):360-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1769963 1769963]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ago, H.]]
[[Category: Ago H]]
[[Category: Fujishima, A.]]
[[Category: Fujishima A]]
[[Category: Katsube, Y.]]
[[Category: Katsube Y]]
[[Category: Kitagawa, Y.]]
[[Category: Kitagawa Y]]
[[Category: Matsuura, Y.]]
[[Category: Matsuura Y]]
[[Category: growth factor]]
 
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Retrieved from "https://proteopedia.org/1bfg"