Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1β

Jiandong Zhang, Lawrence S. Cousens, Phillip J. Barr, Stephen R. Sprang

Research output: Contribution to journalArticlepeer-review

242 Scopus citations

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 Å. bFGF is composed entirely of β-sheet structure, comprising a three-fold repeat of a four-stranded antiparallel β-meander. The topology of bFGF is identical to that of interleukin 1β, 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 β-barrel.

Original languageEnglish
Pages (from-to)3446-3450
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number8
StatePublished - 1991

Keywords

  • Heparin binding site
  • Protein crystallography
  • Receptor recognition

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