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Science 4 January 1991:
Vol. 251. no. 4989, pp. 90 - 93
DOI: 10.1126/science.1702556
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Articles

Science, Vol 251, Issue 4989, 90-93
Copyright © 1991 by American Association for the Advancement of Science

articles

Three-dimensional structures of acidic and basic fibroblast growth factors

X Zhu, H Komiya, A Chirino, S Faham, GM Fox, T Arakawa, BT Hsu, and DC Rees

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.

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.


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