2BFH
CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION
2BFH の概要
| エントリーDOI | 10.2210/pdb2bfh/pdb |
| 分子名称 | BASIC FIBROBLAST GROWTH FACTOR (2 entities in total) |
| 機能のキーワード | growth factor |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14670.92 |
| 構造登録者 | Kitagawa, Y.,Ago, H.,Katsube, Y.,Fujishima, A.,Matsuura, Y. (登録日: 1993-08-31, 公開日: 1994-01-31, 最終更新日: 2024-02-14) |
| 主引用文献 | Ago, H.,Kitagawa, Y.,Fujishima, A.,Matsuura, Y.,Katsube, Y. Crystal structure of basic fibroblast growth factor at 1.6 A resolution. J.Biochem.(Tokyo), 110:360-363, 1991 Cited by PubMed Abstract: We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 A resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson & Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding C alpha atoms being 0.11 A. Their structures are composed of twelve beta-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 beta. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy. PubMed: 1769963主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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