Zhu X, Komiya H, Chirino A, Faham S, Fox G M, Arakawa T, Hsu B T, Rees D C
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
Science. 1991 Jan 4;251(4989):90-3. doi: 10.1126/science.1702556.
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.
成纤维细胞生长因子（FGF）家族的蛋白质成员通过受体介导的途径刺激多种细胞类型的增殖和分化。该家族的两个成员，牛酸性FGF和人碱性FGF的三维结构已通过晶体学方法确定。这些结构包含12条反平行β链，它们以具有近似三重内部对称性的折叠模式排列。之前在大豆胰蛋白酶抑制剂以及白细胞介素-1β和-1α中观察到了拓扑学上等效的折叠。文中给出了FGF中与受体和肝素结合相关的序列位置。这些位点包括β-折叠链10，它与FGF家族几种癌基因蛋白中一个延伸序列插入位点相邻，并且在FGF家族和白细胞介素-1β之间显示出序列保守性。
