1BAR
THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST GROWTH FACTORS
1BAR の概要
エントリーDOI | 10.2210/pdb1bar/pdb |
分子名称 | ACIDIC FIBROBLAST GROWTH FACTOR (2 entities in total) |
機能のキーワード | growth factor |
由来する生物種 | Bos taurus (cattle) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 31579.82 |
構造登録者 | Zhu, X.,Komiya, H.,Chirino, A.,Faham, S.,Fox, G.M.,Arakawa, T.,Hsu, B.T.,Rees, D.C. (登録日: 1992-09-29, 公開日: 1993-10-31, 最終更新日: 2024-02-07) |
主引用文献 | Zhu, X.,Komiya, H.,Chirino, A.,Faham, S.,Fox, G.M.,Arakawa, T.,Hsu, B.T.,Rees, D.C. Three-dimensional structures of acidic and basic fibroblast growth factors. Science, 251:90-93, 1991 Cited by PubMed Abstract: 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. PubMed: 1702556主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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