Crystal structure of basic fibroblast growth factor at 1.6 A 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 & 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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@article{Ago1991CrystalSO, title={Crystal structure of basic fibroblast growth factor at 1.6 A resolution.}, author={Hideo Ago and Yuko Kitagawa and Akinori Fujishima and Yoshiharu Matsuura and Yasuhiro Katsube}, journal={Journal of biochemistry}, year={1991}, volume={110 3}, pages={360-3} }