1g82

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[[Image:1g82.gif|left|200px]]
[[Image:1g82.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1g82", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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{{STRUCTURE_1g82| PDB=1g82 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g82 OCA], [http://www.ebi.ac.uk/pdbsum/1g82 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g82 RCSB]</span>
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'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''
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[[Category: Weich, H.]]
[[Category: Weich, H.]]
[[Category: Yayon, A.]]
[[Category: Yayon, A.]]
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[[Category: fibroblast growth factor]]
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[[Category: Fibroblast growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:15:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:38:40 2008''
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Revision as of 14:15, 2 May 2008

Image:1g82.gif

Template:STRUCTURE 1g82

STRUCTURE OF FIBROBLAST GROWTH FACTOR 9


Overview

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.

About this Structure

1G82 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:11223514 Page seeded by OCA on Fri May 2 17:15:29 2008

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