PT  - JOURNAL ARTICLE
AU  - Zhu, X
AU  - Komiya, H
AU  - Chirino, A
AU  - Faham, S
AU  - Fox, GM
AU  - Arakawa, T
AU  - Hsu, BT
AU  - Rees, DC
TI  - Three-dimensional structures of acidic and basic fibroblast growth factors
AID  - 10.1126/science.1702556
DP  - 1991 Jan 04
TA  - Science
PG  - 90--93
VI  - 251
IP  - 4989
4099  - http://science.sciencemag.org/content/251/4989/90.short
4100  - http://science.sciencemag.org/content/251/4989/90.full
SO  - Science1991 Jan 04; 251
AB  - Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine acidic FGF and human basic FGF, have been crystallographically determined. These structures contain 12 antiparallel beta strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. The locations of sequences implicated in receptor and heparin binding by FGF are presented. These sites include beta-sheet strand 10, which is adjacent to the site of an extended sequence insertion in several oncogene proteins of the FGF family, and which shows sequence conservation among the FGF family and interleukin-1 beta.