Zhang J D, Cousens L S, Barr P J, Sprang S R
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9050.
Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3446-50. doi: 10.1073/pnas.88.8.3446.
The three-dimensional structure of the 146-residue form of human basic fibroblast growth factor (bFGF), expressed as a recombinant protein in yeast, has been determined by x-ray crystallography to a resolution of 1.8 A. bFGF is composed entirely of beta-sheet structure, comprising a three-fold repeat of a four-stranded antiparallel beta-meander. The topology of bFGF is identical to that of interleukin 1 beta, showing that although the two proteins share only 10% sequence identity, bFGF, interleukin 1, and their homologs comprise a family of structurally related mitogenic factors. Analysis of the three-dimensional structure in light of functional studies of bFGF suggests that the receptor binding site and the positively charged heparin binding site correspond to adjacent but separate loci on the beta-barrel.
在酵母中作为重组蛋白表达的146个残基形式的人碱性成纤维细胞生长因子（bFGF）的三维结构已通过X射线晶体学确定，分辨率为1.8埃。bFGF完全由β-折叠结构组成，包含一个由四条反平行β-曲折组成的三重重复结构。bFGF的拓扑结构与白细胞介素1β相同，这表明尽管这两种蛋白质的序列同一性仅为10%，但bFGF、白细胞介素1及其同源物构成了一个结构相关的促有丝分裂因子家族。根据bFGF的功能研究对三维结构进行分析表明，受体结合位点和带正电荷的肝素结合位点对应于β-桶上相邻但分开的位点。
