 |
PDBsum entry 2bfh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Growth factor
|
PDB id
|
|
|
|
2bfh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of basic fibroblast growth factor at 1.6 a resolution.
|
|
|
Authors
|
|
H.Ago,
Y.Kitagawa,
A.Fujishima,
Y.Matsuura,
Y.Katsube.
|
|
|
Ref.
|
|
J Biochem (tokyo), 1991,
110,
360-363.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
