Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces
Abstract
The structure of glycosylated fibroblast growth factor 9 has been determined at 2.6 Å resolution. FGF9 forms dimers with most of the receptor-binding residues buried in the dimer interface.
- Publication:
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Acta Crystallographica Section D
- Pub Date:
- March 2001
- DOI:
- Bibcode:
- 2001AcCrD..57..378H
- Keywords:
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- fibroblast growth factors