PDBsum entry: 1g82

Hormone/growth factor

PDB id: 1g82

Contents

Protein chains

157 a.a. *

Ligands

NAG-NAG-FUC ×3

SO4 ×12

NAG

Waters ×147

* Residue conservation analysis

PDB id:

1g82

Name:

Hormone/growth factor

Title:

Structure of fibroblast growth factor 9

Structure:

Fibroblast growth factor 9. Chain: a, b, c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469. Expression_system_cell_line: sf9.

Biol. unit:

Tetramer (from PQS)

Resolution:

2.60Å R-factor: 0.210 R-free: 0.248

Authors:

H.J.Hecht,R.Adar,B.Hofmann,O.Bogin,H.Weich,A.Yayon

Key ref:

H.J.Hecht et al. (2001). Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces. Acta Crystallogr D Biol Crystallogr, 57, 378-384. PubMed id: 11223514 DOI: 10.1107/S0907444900020813

Date:

16-Nov-00 Release date: 07-Mar-01

Protein chains

P31371  (FGF9_HUMAN) -  Glia-activating factor

Seq: 208 a.a.

Struc: 157 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: growth factor activity (1 term)

DOI no: 10.1107/S0907444900020813

Acta Crystallogr D Biol Crystallogr 57:378-384 (2001)

PubMed id: 11223514

Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.

H.J.Hecht, R.Adar, B.Hofmann, O.Bogin, H.Weich, A.Yayon.

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.

Selected figure(s)

Figure 3.
Figure 3 Hydrogen-bond network stabilizing the 8- 9 loop. Molecule D is represented with a grey chain trace and molecule A with an orange chain trace; hydrogen-bond distances (Å) are shown in red. [Drawn with Molscript (Kraulis, 1991[Kraulis, P. (1991). J. Appl. Cryst. 24, 946-950.]) and rendered with gl_render (L. Esser, unpublished program) and PovRay.]

Figure 4.
Figure 4 Potential heparin-binding sites in FGF9. Chain A is shown in an orientation perpendicular to Fig. 1-as a ribbon representation; the colour code is identical to Fig. 1-. The sulfate-binding residues are shown in ball-and-stick representation and are identified by blue labels. Red labels for primary receptor-binding sites and the glycosylation site (black labels) have been included for reference to Fig. 1-. [Drawn with Molscript (Kraulis, 1991[Kraulis, P. (1991). J. Appl. Cryst. 24, 946-950.]) and rendered with gl_render (L. Esser, unpublished program) and PovRay.]

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 378-384) copyright 2001.

Figures were selected by the author.