1BFG

CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION

Summary for 1BFG

• Entry DOI: 10.2210/pdb1bfg/pdb
• Descriptor: BASIC FIBROBLAST GROWTH FACTOR (2 entities in total)
• Functional Keywords: growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 16403.73

Authors

Kitagawa, Y.,Ago, H.,Katsube, Y.,Fujishima, A.,Matsuura, Y. (deposition date: 1993-04-15, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

Ago, H.,Kitagawa, Y.,Fujishima, A.,Matsuura, Y.,Katsube, Y.
Crystal structure of basic fibroblast growth factor at 1.6 A resolution.
J.Biochem.(Tokyo), 110:360-363, 1991

PubMed Abstract: 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.

PubMed: 1769963

Experimental method

X-RAY DIFFRACTION (1.6 Å)