2bfh: Difference between revisions

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-[[Image:2bfh.jpg|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION==
-|PDB= 2bfh |SIZE=350|CAPTION= <scene name='initialview01'>2bfh</scene>, resolution 2.5&Aring;
+<StructureSection load='2bfh' size='340' side='right'caption='[[2bfh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2bfh]] 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=2BFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFH FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfh OCA], [https://pdbe.org/2bfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfh RCSB], [https://www.ebi.ac.uk/pdbsum/2bfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfh ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfh OCA], [http://www.ebi.ac.uk/pdbsum/2bfh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bfh RCSB]</span>
+[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/2bfh_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=2bfh ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION'''
+==See Also==
+*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
+== References ==
-==Overview==
+<references/>
-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.
+__TOC__
+</StructureSection>
-==About this Structure==
-BFH 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=2BFH OCA].
-==Reference==
-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]
 [[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:05:42 2008''