1G82

STRUCTURE OF FIBROBLAST GROWTH FACTOR 9

Summary for 1G82

• Entry DOI: 10.2210/pdb1g82/pdb
• Descriptor: FIBROBLAST GROWTH FACTOR 9, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
• Functional Keywords: fibroblast growth factor, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 77541.88

Authors

Hecht, H.J.,Adar, R.,Hofmann, B.,Bogin, O.,Weich, H.,Yayon, A. (deposition date: 2000-11-16, release date: 2001-03-07, Last modification date: 2023-08-09)

Primary citation

Hecht, H.J.,Adar, R.,Hofmann, B.,Bogin, O.,Weich, H.,Yayon, A.
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.
Acta Crystallogr.,Sect.D, 57:378-384, 2001

PubMed Abstract: Fibroblast growth factors (FGFs) constitute a family of at least 20 structurally related heparin-binding polypeptides active in regulating cell growth, survival, differentiation and migration. FGF9, originally discovered as a glia-activating factor, shares 30% sequence identity with other FGFs and has a unique spectrum of target-cell specificity. FGF9 crystallized in the tetragonal space group I4(1), with unit-cell parameters a = b = 151.9, c = 117.2 A. The structure of the glycosylated protein has been refined to an R value of 21.0% with R(free) = 24.8%) at 2.6 A resolution. The four molecules in the asymmetric unit are arranged in two non-crystallographic dimers, with the dimer interface composed partly of residues from N- and C-terminal extensions from the FGF core structure. Most of the receptor-binding residues identified in FGF1- and FGF2-receptor complexes are buried in the dimer interface, with the beta8-beta9 loop stabilized in a particular conformation by an intramolecular hydrogen-bonding network. The potential heparin-binding sites are in a pattern distinct from FGF1 and FGF2. The carbohydrate moiety attached at Asn79 has no structural influence.

PubMed: 11223514
DOI: 10.1107/S0907444900020813

Experimental method

X-RAY DIFFRACTION (2.6 Å)