Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta.
The three-dimensional structure of the 146-residue form of human basic fibroblast growth factor (bFGF), expressed as a recombinant protein in yeast, has been determined by x-ray crystallography to a resolution of 1.8 A. bFGF is composed entirely of beta-sheet structure, comprising a three-fold repeat of a four-stranded antiparallel beta-meander. The topology of bFGF is identical to that of interleukin 1 beta, showing that although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally related mitogenic factors. Analysis of the three-dimensional structure in light of functional studies of bFGF suggests that the receptor binding site and the positively charged heparin binding site correspond to adjacent but separate loci on the beta-barrel.
Zhang
J D
JD
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9050.
Cousens
L S
LS
Barr
P J
PJ
Sprang
S R
SR
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003196:Computer Graphics; D003461:Crystallography; D016222:Fibroblast Growth Factor 2 / Q000648:ultrastructure*; D006493:Heparin / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1 / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009841:Oligonucleotides / Q000737:chemistry; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism; D017468:Receptors, Fibroblast Growth Factor; D011994:Recombinant Proteins; D012997:Solvents; D014961:X-Ray Diffraction
D007375:Interleukin-1; D009841:Oligonucleotides; D011956:Receptors, Cell Surface; D017468:Receptors, Fibroblast Growth Factor; D011994:Recombinant Proteins; D012997:Solvents; D016222:Fibroblast Growth Factor 2; D006493:Heparin