2FGF

THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA

2FGF の概要

• エントリーDOI: 10.2210/pdb2fgf/pdb
• 分子名称: HEPARIN-BINDING GROWTH FACTOR 2 PRECURSOR, SULFATE ION (3 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: 16724.05

構造登録者

Zhang, J.,Sprang, S.R. (登録日: 1991-02-19, 公開日: 1992-01-15, 最終更新日: 2024-02-14)

主引用文献

Zhang, J.D.,Cousens, L.S.,Barr, P.J.,Sprang, S.R.
Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta.
Proc.Natl.Acad.Sci.USA, 88:3446-3450, 1991

PubMed Abstract: 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.

PubMed: 1849658
DOI: 10.1073/pnas.88.8.3446

実験手法

X-RAY DIFFRACTION (1.77 Å)