2FGF

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

Summary for 2FGF

• Entry DOI: 10.2210/pdb2fgf/pdb
• Descriptor: HEPARIN-BINDING GROWTH FACTOR 2 PRECURSOR, SULFATE ION (3 entities in total)
• Functional Keywords: growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 16724.05

Authors

Zhang, J.,Sprang, S.R. (deposition date: 1991-02-19, release date: 1992-01-15, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.77 Å)