"Three-dimensional structure of human basic fibroblast growth factor, a" by Jiandong Zhang, Lawrence S. Cousens et al.
 

Document Type

Article

Publication Title

Proceedings of the National Academy of Sciences of the United States of America

Publication Date

4-1991

Volume

88

Disciplines

Biology | Life Sciences

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.

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