X-ray structure and biophysical properties of rabbit fibroblast growth factor 1.
The rabbit is an important and de facto animal model in the study of ischemic disease and angiogenic therapy. Additionally, fibroblast growth factor 1 (FGF-1) is emerging as one of the most important growth factors for novel proangiogenic and pro-arteriogenic therapy. However, despite its significance, the fundamental biophysical properties of rabbit FGF-1, including its X-ray structure, have never been reported. Here, the cloning, crystallization, X-ray structure and determination of the biophysical properties of rabbit FGF-1 are described. The X-ray structure shows that the amino-acid differences between human and rabbit FGF-1 are solvent-exposed and therefore potentially immunogenic, while the biophysical studies identify differences in thermostability and receptor-binding affinity that distinguish rabbit FGF-1 from human FGF-1.
Lee
Jihun
J
Department of Biomedical Sciences, Florida State University, Tallahassee, 32306-4300, USA.
Blaber
Sachiko I
SI
Irsigler
Andre
A
Aspinwall
Eric
E
Blaber
Michael
M
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D005260:Female; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011817:Rabbits; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
D016220:Fibroblast Growth Factor 1