1bfg

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[[Image:1bfg.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION==
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|PDB= 1bfg |SIZE=350|CAPTION= <scene name='initialview01'>1bfg</scene>, resolution 1.6&Aring;
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<StructureSection load='1bfg' size='340' side='right'caption='[[1bfg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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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]] 1.6&#8491;</td></tr>
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|GENE=
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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=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>
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}}
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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/1bfg_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=1bfg ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Cation-pi interactions|Cation-pi interactions]]
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
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==Overview==
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== References ==
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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.
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<references/>
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__TOC__
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==Disease==
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</StructureSection>
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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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==About this Structure==
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1BFG is a [[Single protein]] structure of sequence 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=1BFG OCA].
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==Reference==
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Crystal structure of basic fibroblast growth factor at 1.6 A resolution., Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y, J Biochem. 1991 Sep;110(3):360-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1769963 1769963]
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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: Ago, H.]]
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[[Category: Ago H]]
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[[Category: Fujishima, A.]]
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[[Category: Fujishima A]]
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[[Category: Katsube, Y.]]
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[[Category: Katsube Y]]
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[[Category: Kitagawa, Y.]]
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[[Category: Kitagawa Y]]
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[[Category: Matsuura, Y.]]
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[[Category: Matsuura Y]]
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[[Category: growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:19 2008''
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Current revision

CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION

PDB ID 1bfg

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