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157 a.a.
Key reference
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 the8-
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 and rendered with gl_render (L. Esser, unpublished program) and PovRay.]The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 378-384) copyright 2001.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.
Literature references that cite this PDB file's key reference
PubMed id Reference
19747392 A.L.Roca, Y.Ishida, N.Nikolaidis, S.O.Kolokotronis, S.Fratpietro, K.Stewardson, S.Hensley, M.Tisdale, G.Boeskorov, and A.D.Greenwood (2009).
Genetic variation at hair length candidate genes in elephants and the extinct woolly mammoth.BMC Evol Biol, 9, 232.
19240749 D.Spicer (2009).
FGF9 on the move.Nat Genet, 41, 272-273.
19219044 M.Harada, H.Murakami, A.Okawa, N.Okimoto, S.Hiraoka, T.Nakahara, R.Akasaka, Y.Shiraishi, N.Futatsugi, Y.Mizutani-Koseki, A.Kuroiwa, M.Shirouzu, S.Yokoyama, M.Taiji, S.Iseki, D.M.Ornitz, and H.Koseki (2009).
FGF9 monomer-dimer equilibrium regulates extracellular matrix affinity and tissue diffusion.Nat Genet, 41, 289-298.
15632285 J.Kim, J.Lee, S.R.Brych, T.M.Logan, and M.Blaber (2005).
Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.Protein Sci, 14, 351-359.
PDB codes: 1pzz 1q03 1q04
15382229 M.J.Bernett, T.Somasundaram, and M.Blaber (2004).
An atomic resolution structure for human fibroblast growth factor 1.Proteins, 57, 626-634.
PDB code: 1rg8
12489043 J.C.van Swieten, E.Brusse, B.M.de Graaf, E.Krieger, R.van de Graaf, I.de Koning, A.Maat-Kievit, P.Leegwater, D.Dooijes, B.A.Oostra, and P.Heutink (2003).
A mutation in the fibroblast growth factor 14 gene is associated with autosomal dominant cerebellar ataxia [corrected].Am J Hum Genet, 72, 191-199.
14502551 Y.Luo, H.H.Cho, and W.L.McKeehan (2003).
Biospecific extraction and neutralization of anticoagulant heparin with fibroblast growth factors (FGF).J Pharm Sci, 92, 2117-2127.
11847269 J.Kim, S.I.Blaber, and M.Blaber (2002).
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor.Protein Sci, 11, 459-466.
PDB codes: 1k5u 1k5v The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.
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