Three-dimensional structures of acidic and basic fibroblast growth factors.
Three-dimensional structures of acidic and basic fibroblast growth factors.
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DOI：
10.1126/science.1702556
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发表时间：
1993-10
期刊：
影响因子：
56.9
通讯作者：
Xiaotian Zhu;H. Komiya;A. Chirino;S. Faham;G. M. Fox;T. Arakawa;B. T. Hsu;D. Rees
中科院分区：
文献类型：
--
作者：
Xiaotian Zhu;H. Komiya;A. Chirino;S. Faham;G. M. Fox;T. Arakawa;B. T. Hsu;D. Rees
成纤维细胞生长因子 (FGF) 蛋白家族的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测定。这些结构包含 12 条反向平行的 β 链，它们组织成具有近似三重内部对称的折叠模式。先前已观察到大豆胰蛋白酶抑制剂和白细胞介素-1β和-1α具有拓扑等效的折叠。给出了与 FGF 结合受体和肝素有关的序列位置。这些位点包括 β-折叠链 10，它与 FGF 家族的几个癌基因蛋白中的延伸序列插入位点相邻，并且显示出 FGF 家族和白细胞介素 1 β 之间的序列保守性。
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.