1bfg

<table><tr><td colspan='2'>[[1bfg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='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>

[[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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== Publication Abstract from PubMed ==

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.

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:1769963<ref>PMID:1769963</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bfg" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Ago, H]]

[[Category: Fujishima, A]]

[[Category: Katsube, Y]]

[[Category: Kitagawa, Y]]

[[Category: Matsuura, Y]]

[[Category: Growth factor]]